Lactoperoxidase is a peroxidaseenzyme secreted from mammary, salivary and other mucosal glands including the lungs, bronchii and nose[5] that functions as a natural and the first line of defense against bacteria and viruses.[6] Lactoperoxidase is a member of the heme peroxidase family of enzymes. In humans, lactoperoxidase is encoded by the LPOgene.[7][8]
Lactoperoxidase catalyzes the oxidation of several inorganic and organic substrates by hydrogen peroxide.[9] These substrates include bromide and iodide and therefore lactoperoxidase can be categorised as a haloperoxidase. An other important substrate is thiocyanate. The oxidized products produced through the action of this enzyme have potent and non-specific bactericidal and antiviral activities, including destruction of the influenza virus. Lactoperoxidase together with its inorganic ion substrates, hydrogen peroxide, and oxidized products is known as the lactoperoxidase system.[10] Hence LPO is considered a very important defense against invasive bacteria and viral agents such as influenza and the SARS-CoV-2 virus when sufficient iodine is provided.[11][12][13]
The lactoperoxidase system plays an important role in the innate immune system by killing bacteria in milk and mucosal (linings of mostly endodermal origin, covered in epithelium, which are involved in absorption and secretion) secretions hence augmentation of the lactoperoxidase system may have therapeutic applications. Furthermore, addition or augmentation of the lactoperoxidase system has potential applications in controlling bacteria in food and consumer health care products. The lactoperoxidase system does not attack DNA and is not mutagenic.[14] However, under certain conditions, the lactoperoxidase system may contribute to oxidative stress.[15] Furthermore, lactoperoxidase may contribute to the initiation of breast cancer, through its ability to oxidize estrogenic hormones producing free radical intermediates.[16]
These relatively short lived oxidized intermediates have potent bactericidal effects, hence lactoperoxidase is part of the antimicrobial defense system in tissues that express lactoperoxidase.[10] The lactoperoxidase system is effective in killing a range of aerobic[22] and certain anaerobic microorganisms.[23] Research (1984): "The effect of lactoperoxidase-thiocyanate-hydrogen peroxide mixtures on bacteria is dependent on experimental conditions. If the bacteria are cultured after the exposure to lactoperoxidase-thiocyanate-hydrogen peroxide on nutrient agar under aerobic conditions, they may not grow, whereas they grow readily on blood agar under anaerobic conditions."[24] In its antimicrobial capacity, lactoperoxidase appears to acts synergistically with lactoferrin[25] and lysozyme.[26]
Applications
Lactoperoxidase is an effective antimicrobial and antiviral agent. Consequently, applications of lactoperoxidase are being found in preserving food, cosmetics, and ophthalmic solutions. Furthermore, lactoperoxidase have found application in dental and wound treatment. Finally lactoperoxidase may find application as anti-tumor and anti viral agents.[27] Lactoperoxidase has been used with radioactive iodine to selectively label membrane surfaces.[28]
Dairy products
Lactoperoxidase is an effective antimicrobial agent and is used as an antibacterial agent in reducing bacterial microflora in milk and milk products.[29] Activation of the lactoperoxidase system by addition of hydrogen peroxide and thiocyanate extends the shelf life of refrigerated raw milk.[19][30][31][32] It is fairly heat resistant and is used as an indicator of overpasteurization of milk.[33]
Oral care
A lactoperoxidase system is claimed to appropriate for the treatment of gingivitis and paradentosis.[34] Lactoperoxidase has been used in toothpaste or a mouthrinse to reduce oral bacteria and consequently the acid produced by those bacteria.[35]
Cosmetics
A combination of lactoperoxidase, glucose, glucose oxidase (GOD), iodide and thiocyanate is claimed to be effective in the preservations of cosmetics.[36]
Cancer
Antibody conjugates of glucose oxidase and to lactoperoxidase have been found to effective in killing tumor cells in vitro.[37] In addition, macrophages exposed to lactoperoxidase are stimulated to kill cancer cells.[38] Knockout mice deficient in lactoperoxidase suffer ill-health and develop tumors.[39]
Clinical significance
Innate immune system
The antibacterial and anti-viral activities of lactoperoxidase play an important role in the mammalian immune defense system; the lactoperoxidase system is considered the first line of defense against airborne bacteria and viral agents.[40][41][42] Importantly, lactoperoxidase is also extruded into the lung, bronchii and nasal mucus.[43]
Hypothiocyanite is one of the reactive intermediates produced by the activity of lactoperoxidase on thiocyanate and hydrogen peroxide produced by dual oxidase 2 proteins, also known as Duox2.[44][45] Thiocyanate secretion[46] in cystic fibrosis patients is decreased, resulting in a reduced production of the antimicrobial hypothiocyanite and consequently contributes to increased risk of airway infection.[47][48]
Viral infections
Peroxidase-generated hypoiodous acid (HOI), hypoiodite and hypothiocyanite all destroy the herpes simplex virus[49] and human immunodeficiency virus.[50] Both the hypothiocyanite and the hypoiodate ion products are very potent and importantly non-specific antiviral oxidants which are lethal, even in small concentrations, to the influenza virus.[51] The anti-viral activity of lactoperoxidase is enhanced with increasing concentrations of iodide ion.[52] This enzyme has been shown effective against a highly dangerous and tough RNA virus (poliovirus) and a long-lived DNA virus (vaccina).[53]
Bacterial infections
The duox2-lactoperoxidase system has been shown to offer protection against many dozens of bacteria and mycoplasmas including varieties of the clinically important Staphylococcus and many Streptococcus types.[54] The lactoperoxidase system efficiently inhibits the common helicobacter pylori in buffer; however, in whole human saliva, it seems to have a weaker effect against this microbe.[55] It has been shown that lactoperoxidase in the presence of thiocyanide can catalyze the bactericidal and cytotoxic effects of hydrogen peroxide under specific conditions when hydrogen peroxide is present in excess of thiocyanide.[24] The combination of lactoperoxidase, hydrogen peroxide and thiocyanide is much more effective than hydrogen peroxide alone to inhibit bacterial metabolism and growth.[56]
Breast cancer
The oxidation of estradiol by lactoperoxidase is a possible source of oxidative stress in breast cancer.[15][16] The ability of lactoperoxidase to propagate a chain reaction leading to oxygen consumption and intracellular hydrogen peroxide accumulation could explain the hydroxyl radical-induced DNA base lesions recently reported in female breast cancer tissue.[15] Lactoperoxidase may be involved in breast carcinogenesis, because of its ability to interact with estrogenic hormones and oxidise them through two one-electron reaction steps.[16] Lactoperoxidase reacts with the phenolic A-ring of estrogens to produce reactive free radicals.[57] In addition, lactoperoxidase may activate carcinogenic aromatic and heterocyclic amines and increase binding levels of activated products to DNA, which suggests a potential role of lactoperoxidase-catalyzed activation of carcinogens in the causation of breast cancer.[58]
Oral Care
During the last decades, several clinical studies describing the clinical efficacy of the lactoperoxidase system in a variety of oral care products (tooth pastes, mouth rinses) have been published. After showing indirectly, by means of measuring experimental gingivitis and caries parameters, that mouth rinses[59][60] containing amyloglucosidase (γ-amylase) and glucose oxidase activate the lactoperoxidase system, the protective mechanism of the enzymes in oral care products has been partially elucidated. Enzymes such as lysozyme, lactoperoxidase and glucose oxidase are transferred from the tooth pastes to the pellicle. Being components of the pellicle, these enzymes are catalytically highly active.[61][62] Also, as part of tooth pastes, the lactoperoxidase system has a beneficial influence to avoid early childhood caries[63] by reducing the number of colonies formed by the cariogenic microflora while increasing the thiocyanate concentration. With xerostomia patients, tooth pastes with the lactoperoxidase system are seemingly superior to fluoride-containing tooth pastes with respect to plaque formation and gingivitis.[64] More studies are required[62] to examine further the protective mechanisms.[65]
The application of lactoperoxidase is not restricted to caries, gingivitis, and periodontitis.[66] A combination of lysozyme and lactoperoxidase can be applied to support the treatment of the burning mouth syndrome (glossodynia). In combination with lactoferrin, lactoperoxidase combats halitosis;[67] in combination with lactoferrin and lysozyme, lactoperoxidase helps to improve symptoms of xerostomia.[68] Furthermore, gels with lactoperoxidase help to improve symptoms of oral cancer when saliva production is compromised due to irradiation. In this case, also the oral bacterial flora are influenced favorably.[69][70][71]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Tenovuo JO (1985). "The peroxidase system in human secretions". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN978-0-8247-7298-7.
^Pruitt KM, Reiter B (1985). "Biochemistry of peroxidase systems: antimicrobial effects". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN978-0-8247-7298-7.
^Dull TJ, Uyeda C, Strosberg AD, Nedwin G, Seilhamer JJ (September 1990). "Molecular cloning of cDNAs encoding bovine and human lactoperoxidase". DNA and Cell Biology. 9 (7): 499–509. doi:10.1089/dna.1990.9.499. PMID2222811.
^Kiser C, Caterina CK, Engler JA, Rahemtulla B, Rahemtulla F (September 1996). "Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA". Gene. 173 (2): 261–4. doi:10.1016/0378-1119(96)00078-9. PMID8964511.
^Kohler H, Jenzer H (1989). "Interaction of lactoperoxidase with hydrogen peroxide. Formation of enzyme intermediates and generation of free radicals". Free Radical Biology & Medicine. 6 (3): 323–39. doi:10.1016/0891-5849(89)90059-2. PMID2545551.
^ abTenovuo JO, Pruitt KM, eds. (1985). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN978-0-8247-7298-7.
^ abcSipe HJ, Jordan SJ, Hanna PM, Mason RP (November 1994). "The metabolism of 17 beta-estradiol by lactoperoxidase: a possible source of oxidative stress in breast cancer". Carcinogenesis. 15 (11): 2637–43. doi:10.1093/carcin/15.11.2637. PMID7955118.
^Singh AK, Smith ML, Yamini S, Ohlsson PI, Sinha M, Kaur P, et al. (October 2012). "Bovine carbonyl lactoperoxidase structure at 2.0Å resolution and infrared spectra as a function of pH". The Protein Journal. 31 (7): 598–608. doi:10.1007/s10930-012-9436-3. PMID22886082. S2CID22945713.
^PDB: 2r5l; Singh AK, Singh N, Sharma S, Singh SB, Kaur P, Bhushan A, et al. (February 2008). "Crystal structure of lactoperoxidase at 2.4 A resolution". Journal of Molecular Biology. 376 (4): 1060–75. doi:10.1016/j.jmb.2007.12.012. PMID18191143.
^ abde Wit JN, van Hooydonk AC (1996). "Structure, functions and applications of lactoperoxidase in natural antimicrobial systems". Netherlands Milk & Dairy Journal. 50: 227–244.
^Wever R, Kast WM, Kasinoedin JH, Boelens R (December 1982). "The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 709 (2): 212–9. doi:10.1016/0167-4838(82)90463-0. PMID6295491.
^Pruitt KM, Tenovuo J, Andrews RW, McKane T (February 1982). "Lactoperoxidase-catalyzed oxidation of thiocyanate: polarographic study of the oxidation products". Biochemistry. 21 (3): 562–7. doi:10.1021/bi00532a023. PMID7066307.
^Courtois P, Majerus P, Labbé M, Vanden Abbeele A, Yourassowsky E, Pourtois M (September 1992). "Susceptibility of anaerobic microorganisms to hypothiocyanite produced by lactoperoxidase". Acta Stomatologica Belgica. 89 (3): 155–62. PMID1481764.
^Reiter B (1983). "The biological significance of lactoferrin". International Journal of Tissue Reactions. 5 (1): 87–96. PMID6345430.
^Roger V, Tenovuo J, Lenander-Lumikari M, Söderling E, Vilja P (1994). "Lysozyme and lactoperoxidase inhibit the adherence of Streptococcus mutans NCTC 10449 (serotype c) to saliva-treated hydroxyapatite in vitro". Caries Research. 28 (6): 421–8. doi:10.1159/000262015. PMID7850845.
^Harper WJ (2000). Biological properties of whey components a review. Chicago, IL: American Dairy Products Institute. p. 54.
^Reiter B.; Härnulv BG. "The preservation of refrigerated and uncooled milk by its natural lactoperoxidase system". Dairy Ind. Int. 47 (5): 13–19.
^Zajac M, Glandys J, Skarzynska M, Härnulv G, Eilertsen K (1983). "Milk quality preservation by heat treatment or activation of the lactoperoxidase system in combination with refrigerated storage". Milchwissenschaft. 38 (11).
^Korhonen H (1980). "A new method for preserving raw milk: The lactoperoxidase antibacterial system". World Anim. Rev. 35: 23–29.
^Marks NE, Grandison AS, Lewis MJ (2008). "Use of hydrogen peroxide detection strips to determine the extent of pasteurization in whole milk". International Journal of Dairy Technology. 54 (1): 20–22. doi:10.1046/j.1471-0307.2001.00008.x.
^WO application WO1988002600, Poulson OM, "Enzyme-containing bactericidal composition, and dental and wound treatment preparations comprising this composition", published 1988-04-21
^Hoogedoorn H (1985). "Activation of the salivary peroxidase system: clinical studies". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. pp. 217–228. ISBN978-0-8247-7298-7.
^US 5607681, Galley E, Godfrey DC, Guthrie WG, Hodgkinson DM, Linnington HL, "Antimicrobial Compositions Containing Iodide, Thiocyanate, Glucose And Glucose Oxidase", published 1997-03-04, assigned to The Boots Company PLC
^Stanislawski M, Rousseau V, Goavec M, Ito H (October 1989). "Immunotoxins containing glucose oxidase and lactoperoxidase with tumoricidal properties: in vitro killing effectiveness in a mouse plasmacytoma cell model". Cancer Research. 49 (20): 5497–504. PMID2790777.
^Lefkowitz DL, Hsieh TC, Mills K, Castro A (1990). "Induction of tumor necrosis factor and cytotoxicity by macrophages exposed to lactoperoxidase and microperoxidase". Life Sciences. 47 (8): 703–9. doi:10.1016/0024-3205(90)90625-2. PMID2402192.
^Wijkstrom-Frei C, El-Chemaly S, Ali-Rachedi R, Gerson C, Cobas MA, Forteza R, et al. (August 2003). "Lactoperoxidase and human airway host defense". American Journal of Respiratory Cell and Molecular Biology. 29 (2): 206–12. CiteSeerX10.1.1.325.1962. doi:10.1165/rcmb.2002-0152OC. PMID12626341.
^Conner GE, Salathe M, Forteza R (December 2002). "Lactoperoxidase and hydrogen peroxide metabolism in the airway". American Journal of Respiratory and Critical Care Medicine. 166 (12 Pt 2): S57-61. doi:10.1164/rccm.2206018. PMID12471090.
^Thomas EL, Bates KP, Jefferson MM (September 1980). "Hypothiocyanite ion: detection of the antimicrobial agent in human saliva". Journal of Dental Research. 59 (9): 1466–72. doi:10.1177/00220345800590090201. PMID6931123. S2CID7717994.
^Mikola H, Waris M, Tenovuo J (March 1995). "Inhibition of herpes simplex virus type 1, respiratory syncytial virus and echovirus type 11 by peroxidase-generated hypothiocyanite". Antiviral Research. 26 (2): 161–71. doi:10.1016/0166-3542(94)00073-H. PMID7605114.
^Pourtois M, Binet C, Van Tieghem N, Courtois PR, Vandenabbeele A, Thirty L (May 1991). "Saliva can contribute in quick inhibition of HIV infectivity". AIDS. 5 (5): 598–600. doi:10.1097/00002030-199105000-00022. PMID1650564.
^Tenovuo JO (1985). "Biochemistry of Peroxidase System: Antimicrobial Effects". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN978-0-8247-7298-7.
^Gorlewska-Roberts KM, Teitel CH, Lay JO, Roberts DW, Kadlubar FF (December 2004). "Lactoperoxidase-catalyzed activation of carcinogenic aromatic and heterocyclic amines". Chemical Research in Toxicology. 17 (12): 1659–66. doi:10.1021/tx049787n. PMID15606142.
^Hugoson A, Koch G, Thilander H, Hoogendoorn H (1974). "Lactoperoxidase in the prevention of plaque accumulation, gingivitis and dental caries. 3. Effect of mouthrinses with amyloglucosidase and glucoseoxidase in the model system of experimental gingivitis and caries in man". Odontologisk Revy. 25 (1): 69–80. PMID4522423.
^Hannig C, Spitzmüller B, Lux HC, Altenburger M, Al-Ahmad A, Hannig M (July 2010). "Efficacy of enzymatic toothpastes for immobilisation of protective enzymes in the in situ pellicle". Archives of Oral Biology. 55 (7): 463–9. doi:10.1016/j.archoralbio.2010.03.020. PMID20417500.
^Jyoti S, Shashikiran ND, Reddy VV (2009). "Effect of lactoperoxidase system containing toothpaste on cariogenic bacteria in children with early childhood caries". The Journal of Clinical Pediatric Dentistry. 33 (4): 299–303. doi:10.17796/jcpd.33.4.83331867x68w120n. PMID19725235.
^van Steenberghe D, Van den Eynde E, Jacobs R, Quirynen M (April 1994). "Effect of a lactoperoxidase containing toothpaste in radiation-induced xerostomia". International Dental Journal. 44 (2): 133–8. PMID8063434.
^Kirstilä V, Lenander-Lumikari M, Tenovuo J (December 1994). "Effects of a lactoperoxidase-system-containing toothpaste on dental plaque and whole saliva in vivo". Acta Odontologica Scandinavica. 52 (6): 346–53. doi:10.3109/00016359409029032. PMID7887144.
^Gil-Montoya JA, Guardia-López I, González-Moles MA (March 2008). "Evaluation of the clinical efficacy of a mouthwash and oral gel containing the antimicrobial proteins lactoperoxidase, lysozyme and lactoferrin in elderly patients with dry mouth--a pilot study". Gerodontology. 25 (1): 3–9. doi:10.1111/j.1741-2358.2007.00197.x. PMID18194332.
^Nagy K, Urban E, Fazekas O, Thurzo L, Nagy E (September 2007). "Controlled study of lactoperoxidase gel on oral flora and saliva in irradiated patients with oral cancer". The Journal of Craniofacial Surgery. 18 (5): 1157–64. doi:10.1097/scs.0b013e3180de6311. PMID17912104. S2CID1253647.
^Matear DW, Barbaro J (January 2005). "Effectiveness of saliva substitute products in the treatment of dry mouth in the elderly: a pilot study". The Journal of the Royal Society for the Promotion of Health. 125 (1): 35–41. doi:10.1177/146642400512500113. PMID15712851. S2CID36508570.
Ekstrand B (1994). "Lactoperoxidase and lactoferrin". In Beuchat LR, Dillon VM, Board RG (eds.). Natural antimicrobial systems and food preservation. Oxon: CAB International. ISBN978-0-85198-878-8.
Korhonen H, Meriläinen V, Antila M, Kouvalainen K (1980). "[Antimicrobial factors in milk and infection resistance in infants]". Duodecim; Laaketieteellinen Aikakauskirja (in Finnish). 96 (3): 184–99. PMID7192622.
Hannuksela S, Tenovuo J, Roger V, Lenander-Lumikari M, Ekstrand J (1994). "Fluoride inhibits the antimicrobial peroxidase systems in human whole saliva". Caries Research. 28 (6): 429–34. doi:10.1159/000262016. PMID7850846.
Aune TM, Thomas EL (March 1978). "Oxidation of protein sulfhydryls by products of peroxidase-catalyzed oxidation of thiocyanate ion". Biochemistry. 17 (6): 1005–10. doi:10.1021/bi00599a010. PMID204336.
Dorysthenes rostratus Klasifikasi ilmiah Kerajaan: Animalia Filum: Arthropoda Kelas: Insecta Ordo: Coleoptera Famili: Cerambycidae Genus: Dorysthenes Spesies: Dorysthenes rostratus Dorysthenes rostratus adalah spesies kumbang tanduk panjang yang tergolong famili Cerambycidae. Spesies ini juga merupakan bagian dari genus Dorysthenes, ordo Coleoptera, kelas Insecta, filum Arthropoda, dan kingdom Animalia. Larva kumbang ini biasanya mengebor ke dalam kayu dan dapat menyebabkan kerusakan pada ba...
Jeux olympiques d'été de 1996 Localisation Pays hôte États-Unis Ville hôte Atlanta Date Du 19 juillet au 4 août 1996 Ouverture officielle par Bill ClintonPrésident des États-Unis Participants Pays 197 Athlètes 10 318(6 806 masc. et 3 512 fém.) Compétition Nouveaux sports Softball, Beach-volley et VTT. Nombre de sports 26 Nombre de disciplines 37 Épreuves 271 Symboles Serment olympique Teresa EdwardsJoueuse de basket-ball Flamme olympique Mohamed AliBoxeur américai...
Pengadilan adat kuno di Tomok, Pulau Samosir, Sumatera Utara Pengadilan di Kutaraja (kini Banda Aceh) pada tahun 1903 Pengadilan atau mahkamah adalah instansi resmi yang melaksanakan keadilan dan sistem peradilan serta pengadilan itu sendiri berupa memeriksa hasil penyelidikan Polri, Tipikor, KPK dalam pembuktian gugatan dan juga sanggahan dari tergugat mengadili hingga memutuskan[1]. Sedangkan Mahkamah Agung Republik Indonesia (MA) ialah suatu lembaga tinggi negara yang melaksanakan ...
2004 single by John MayerDaughtersSingle by John Mayerfrom the album Heavier Things B-sideCome Back to Bed, Home LifeReleasedSeptember 28, 2004Length3:59LabelColumbiaSongwriter(s)John MayerProducer(s)Jack Joseph PuigJohn Mayer singles chronology Clarity (2004) Daughters (2004) Go! (2005) Music videoJohn Mayer - Daughters on YouTube Daughters John Mayer's Daughters from Heavier Things Problems playing this file? See media help. Daughters is the third single from Heavier Things, the 2003 studi...
Body responsible for election procedures in Iran Election OfficeElection commission overviewJurisdictionIranHeadquartersTehran, IranMinister responsibleAhmad Vahidi, MinisterElection commission executiveMohammad-Taghi Shahcheraghi [1], HeadParent departmentMinistry of Interior The Election Office (Persian: ستاد انتخابات کشور) is the body charged for implementation of election procedures in Iran and is subordinate to the Ministry of Interior.[2] List of Heads Th...
Portion of Turkey that is located in Southeast Europe European Turkey redirects here. For the Ottoman lands historically known as Turkey in Europe, see Rumelia. East Thrace (blue) within Thrace (yellow)East Thrace (blue) within the Marmara Region of Turkey East Thrace landscape in Edirne Province, Turkey East Thrace or Eastern Thrace (Turkish: Doğu Trakya or simply Trakya; Greek: Ανατολική Θράκη, romanized: Anatolikí Thráki; Bulgarian: Източна Тракия, romani...
معاهدة الصداقة بين اليمن وهولندا المملكة المتوكلية اليمنية مملكة هولندا المساحة (كم)2 195000 42201 عاصمة صنعاء أمستردام لغة رسمية العربية الهولندية نظام الحكم ملكية مطلقة ملكية دستورية تعديل مصدري - تعديل معاهدة الصداقة بين اليمن وهولندا وقعت في صنعاء بين المم...
New Zealand politician (born 1934) For other uses, see Bill Birch (disambiguation). The Right HonourableSir William BirchGNZM38th Minister of FinanceIn office22 June 1999 – 10 December 1999Prime MinisterJenny ShipleyPreceded byBill EnglishSucceeded byMichael CullenIn office29 November 1993 – 31 January 1999Prime MinisterJim Bolger Jenny ShipleyPreceded byRuth RichardsonSucceeded byBill English2nd Treasurer of New ZealandIn office14 August 1998 – 22 June 1999Pr...
Class of fishes Lobe-finned fishesTemporal range: Late Silurian–Present, 425–0 Ma[1] PreꞒ Ꞓ O S D C P T J K Pg N From top to bottom and left to right, examples of sarcopterygians: Guiyu oneiros, West Indian Ocean coelacanth, Australian lungfish and the tetrapodomorph Panderichthys rhombolepis. Scientific classification Domain: Eukaryota Kingdom: Animalia Phylum: Chordata Superclass: Osteichthyes Clade: SarcopterygiiRomer, 1955 Subgroups ?†Psarolepids Guiyu Sparalepis Ps...
American comedy musician (born 1959) For the album, see Weird Al Yankovic (album). Weird Al YankovicYankovic performing in 2010Background informationBirth nameAlfred Matthew YankovicBorn (1959-10-23) October 23, 1959 (age 64)Downey, California, U.S.OriginLynwood, California, U.S.Genres Comedy parody polka geek rock[1] Occupations Singer songwriter musician record producer actor parodist author Instruments Vocals accordion keyboards DiscographyWeird Al Yankovic discographyYears ac...
Hindu temple in Kerala, India This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed.Find sources: Kadakkal Devi Temple – news · newspapers · books · scholar · JSTOR (June 2009) (Learn how and when to remove this message) Kadakkal Devi Temple is situated at Kollam District, Kerala, India. Kadakkal village is in the eastern part ...
توليو ليفي تشيفيتا توليو ليفي تشيفيتا معلومات شخصية الميلاد 29 مارس 1873(1873-03-29)بادوفا، إيطاليا الوفاة 29 ديسمبر 1941 (68 سنة)روما، إيطاليا الجنسية إيطالي العرق يهودي [1] عضو في الجمعية الملكية، وأكاديمية العلوم في الاتحاد السوفيتي، وأكاديمية سانت بطرسبرغ للعلوم ...
Fatty seed of Theobroma cacao For other uses of Cacao, see Cacao (disambiguation). Forms of the cocoa bean during productionPods at various stages of ripeningBeans in pulp in freshly cut podBeans: In pulp, in skin, and nakedRoasted nibs (pieces of kernels) are generally powdered and melted into chocolate liquor, but also inserted into chocolate bars to give additional crunch. The cocoa bean, also known simply as cocoa (/ˈkoʊ.koʊ/) or cacao (/kəˈkaʊ/),[1] is the dried and fully f...
Schloss Kaufungen Schloss Kaufungen Schloss Kaufungen Staat Deutschland Ort Wolkenburg-Kaufungen Entstehungszeit um 1530 Erhaltungszustand erhalten Ständische Stellung Adlige Geographische Lage 50° 53′ N, 12° 41′ O50.89059312.681437Koordinaten: 50° 53′ 26,1″ N, 12° 40′ 53,2″ O Schloss Kaufungen (Sachsen) p3 Das Schloss Kaufungen ist ein Schloss in der Ortslage Kaufungen im Ortsteil Wolkenburg-Kaufungen der Stadt Limbach-...
This list is incomplete; you can help by adding missing items. (September 2012) This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed.Find sources: List of cases of police brutality in India – news · newspapers · books · scholar · JSTOR (December 2013) (Learn how and when to remove this message) This is a list of notable cases...
Mary TudorPermaisuri Raja PrancisPeriode9 Oktober 1514 – 1 Januari 1515Penobatan5 November 1514Kelahiran(1496-03-18)18 Maret 1496Istana Richmond, SurreyKematian25 Juni 1533(1533-06-25) (umur 37)Balai Westhorpe, SuffolkPemakamanGereja Santa Maria, Bury St. EdmundsPasanganLouis XII, Raja PrancisCharles Brandon, Adipati SuffolkKeturunanHenry BrandonFrances GreyEleanor CliffordHenry BrandonWangsaTudorAyahHenry VII, Raja InggrisIbuElizabeth dari YorkAgamaKatolik Roma Mary Tudor (18 Maret 14...