Derleme
BibTex RIS Kaynak Göster
Yıl 2019, Cilt: 2 Sayı: 4, 224 - 229, 01.10.2019

Öz

Kaynakça

  • Alım Z, Beydemir Ş. 2012. Effects of some anti-neoplastic drugs on sheep liver sorbitol Dehydrogenase. Physiol Biochem, 118(5): 244- 252.
  • Bohren KM, Bullock B, Wermuth B, Gabbay KH. 1989. The aldoketo reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem, 264: 9547-9551.
  • Burnett AL. 1997. Nitric oxide in the penis: Physiology and pathology. J Urol, 157:320-324.
  • C. Yabe-Nishimura. 1998. Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications. Pharmacol Rev, 50(1): 21– 34.
  • Cama E. 2003. Human arginase II: Crystal structure and physiological role in male an female sexual arousal. Biochem, 42:8445-8451.
  • Cantor, AH. 1997. The role of selenium in poultry nutrition. Biotechnology in the feed industry, proceedings of Alltechs thirteen annual symposium edited by TP Lyons and KA Jacques.
  • Çetin M, Deniz G, Polat Ü ve Yalçın A. 2002. Broylerlerde inorganik ve organik selenyum ilavesinin biyokimyasal kan parametreleri üzerine etkisi Uludağ Üniv J Fac Med 21: 59-63.
  • Cook HT, Jansen A, Lewis S, Largen P, O’Donnell M, Reaveley D, Cattel V. 1994. Arginine metabolism in experimental glomerulonephritis: Interaction between nitric oxide synthase and arginase.
  • Del Corso A, Costantino L, Rastelli G, Buono F and Mura U. 2000. Aldose reductase does catalyse the reduction of glyceraldehyde through a stoichiometric oxidation of NADPH. Experiment Eye Res, 71: 515-521.
  • Eaton, DL and TK Bammler 1999. Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol Sciences, 49 (2): 156-164.
  • Flouriot G, Vaillant C, Salbert G, Pelisserro C, Guiraud JM, Valotaire Y. 1993. Monolayer and aggregate cultures of rainbow trout hepatocytes: long-term and stable liver-spesific expression in aggregates. J Cell Sci, 105: 407-416.
  • Flynn TG, Shires J, Walton DJ. 1975. Properties of the nicotinamide adenine dinucleotide phosphate-dependent aldehyde reductase from pig kidney: amino acid composition, reactivity of cysteinyl residues, and stereochemistry of Dglyceraldehyde reduction. JBC 250: 2933–2940.
  • Greenberg DM. 1960. Enzymes of urea cycle. In: Enzymes, Boyer PD, Lardy H, Myrback K (Eds), Academic Press, N Y.
  • Hers H. 1956. The mechanism of the transformation of glucose in fructose in the seminal vesicles. Biochimica Biophysica Acta, 22(1): 202-203.
  • Holyle CHV, Stones RW, Robson T, Whitel YK, Burnstock G. 1996. Innervation of vasculature and microvasculature of the human vagina by NOS and neuropeptide- containing nerves. J Anat, 186: 633-644.
  • Hoshi A, Takahashi M, Fujii J, Myint T, Kaneto H, Suzuki K, Yamasaki Y, Kamada T, Taniguchi N. 1996. Glycation and inactivation of sorbitol dehydrogenase in normal and diabetic rats. Biochem J, 318: 119-123.
  • Ireland JJ, Murphee RL, Coulson PB. 1980. Accuracy of predicting stages of bovine estrous cycle by gross appearance of the corpus luteum. J Dairy Sci, 63: 155-160.
  • Jeffery J, Jornvall H. 1988. Sorbitol dehydrogenase. Advances in. Enzymol, 61: 47-106.
  • Johansson K, El-Ahmad M, Kaiser C, Jornvall H, Eklund H, Hoog, JO, 2001. Crystal structure of sorbitol dehydrogenase. Chem Biol Interact, 130: 351-358.
  • Kador PF, Kinoshita JH, Stribling D, Brittain DR, Mirrless DJ, Sennitt CM. 1987. Rat lens aldose reductase and poliol production. Biochem J, 247:495-496.
  • Kocna P, Fric P, Zavoral M, Pelech T. 1996. Arginase activity determination. A marker of large bowel mucosal proliferation. Eur J Clin Biochem, 34: 619–623.
  • Latonelle K, Le Menn F, Kaushik S, J, Pelissero C, B, 2002. Effects of dietary phytoestrogens in vivo and in vitro in rainbow trout and siberian sturgeon: interests and limits of the in vitro studies of interspecies differences. General and Comparative Endocrinology, 126: 39-51.
  • Nishimura C, Matsuura Y, Kokai Y, Akera T, Carper D, Morjana, N. 1990. Cloning and expression of human aldose reductase. J Biol Chem, 265: 9788-9792.
  • Razmi N, Jelodar GA, Nazifi S, Dehghani A. 2005. Arginase status in cattle reproductive system. Vet Arhiv, 75:31-38.
  • Razmi N, Jelodar GA, Nazifi S, Dehghani A. 2005. Arginase status in cattle reproductive system. Vet Arhiv, 75: 31-38.
  • Reiersen H, Lindstad, RI, Mckinley-Mckee, JS. 1994. The inactivation of sheep liver sorbitol dehydrogenase by pyrophosphate and some analogous metal chelators. Biochem Biophys, 311: 450-456.
  • Takahashi M, Fujii J, Teshima T, Suzuki K, Shiba T, Taniguchi N. 1993. Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression. Gene, 127: 249-253.
  • Tanimoto T, Maekawa K, Okada S, Yabe Nishimura C. 1998. Clinical analysis of aldose reductase for differential diagnosis of the pathogenesis of diabetic complication. Analytica Chimica Acta, 365: 285-292.
  • Underwood, EJ, Stuttle, NF. 1999. The mineral nutrition of livestock. Selenium. CAB International Wallingford, UK, 421- 474.
  • Wermuth B, Munch, JD and Von Wartburg, JP. 1977. Purification and properties of NADPH-dependent aldehyde reductase from human liver. JBC, 252:3821–3828.
  • Wilson L. 2003. Arginase inhibitors touted as potential drug target for sexual dysfunction. Biochem, 81: 9.
  • Yallampalli C, Dongy YL. 2000. Estradiol-17 inhibits nitric oxide synthase (NOS)-II and stimulates NOS-III gene expression in the rat uterus. Biol Reprod, 63:34-41.
  • Yu H, Yoo PK, Aguirre CC, Tsoa RW, Kern RM, Grody WW. 2003. Widespread expression of arginase I in mouse tissues: Biochemical and physiological implications. J Histoch Cytoch, 51: 1151–1160.
  • Yüksel M, Kandemir FM, Deveci H, Özdemir N. 2012. İneklerde seksüel siklusun farklı dönemlerinde uterus arginaz seviyelerinin araştırılması. YYÜ Vet Fak Derg 23(1): 15-17.

The Enzymes That Affect the Reproduction in Certain Farm Animals

Yıl 2019, Cilt: 2 Sayı: 4, 224 - 229, 01.10.2019

Öz

The study was carried out to determine the enzymes that affect the reproduction in certain farm animals.
Studies of cattle, sheep, chicken and fish as animal species were examined. Researches of holstein, simmental and
montofon from different cattle breeds, in addition, as fish specie sea bream (Sparus aurata L.) were mentioned. The
levels of Glutathione S-transferase and uterine arginase in cattle, sorbitol dehydrogenase and aldose reductase in
sheep, Glutathione peroxidase in chicken and aromatase in sea bream effect on reproduction and reproductive
performance were researched.

Kaynakça

  • Alım Z, Beydemir Ş. 2012. Effects of some anti-neoplastic drugs on sheep liver sorbitol Dehydrogenase. Physiol Biochem, 118(5): 244- 252.
  • Bohren KM, Bullock B, Wermuth B, Gabbay KH. 1989. The aldoketo reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem, 264: 9547-9551.
  • Burnett AL. 1997. Nitric oxide in the penis: Physiology and pathology. J Urol, 157:320-324.
  • C. Yabe-Nishimura. 1998. Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications. Pharmacol Rev, 50(1): 21– 34.
  • Cama E. 2003. Human arginase II: Crystal structure and physiological role in male an female sexual arousal. Biochem, 42:8445-8451.
  • Cantor, AH. 1997. The role of selenium in poultry nutrition. Biotechnology in the feed industry, proceedings of Alltechs thirteen annual symposium edited by TP Lyons and KA Jacques.
  • Çetin M, Deniz G, Polat Ü ve Yalçın A. 2002. Broylerlerde inorganik ve organik selenyum ilavesinin biyokimyasal kan parametreleri üzerine etkisi Uludağ Üniv J Fac Med 21: 59-63.
  • Cook HT, Jansen A, Lewis S, Largen P, O’Donnell M, Reaveley D, Cattel V. 1994. Arginine metabolism in experimental glomerulonephritis: Interaction between nitric oxide synthase and arginase.
  • Del Corso A, Costantino L, Rastelli G, Buono F and Mura U. 2000. Aldose reductase does catalyse the reduction of glyceraldehyde through a stoichiometric oxidation of NADPH. Experiment Eye Res, 71: 515-521.
  • Eaton, DL and TK Bammler 1999. Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol Sciences, 49 (2): 156-164.
  • Flouriot G, Vaillant C, Salbert G, Pelisserro C, Guiraud JM, Valotaire Y. 1993. Monolayer and aggregate cultures of rainbow trout hepatocytes: long-term and stable liver-spesific expression in aggregates. J Cell Sci, 105: 407-416.
  • Flynn TG, Shires J, Walton DJ. 1975. Properties of the nicotinamide adenine dinucleotide phosphate-dependent aldehyde reductase from pig kidney: amino acid composition, reactivity of cysteinyl residues, and stereochemistry of Dglyceraldehyde reduction. JBC 250: 2933–2940.
  • Greenberg DM. 1960. Enzymes of urea cycle. In: Enzymes, Boyer PD, Lardy H, Myrback K (Eds), Academic Press, N Y.
  • Hers H. 1956. The mechanism of the transformation of glucose in fructose in the seminal vesicles. Biochimica Biophysica Acta, 22(1): 202-203.
  • Holyle CHV, Stones RW, Robson T, Whitel YK, Burnstock G. 1996. Innervation of vasculature and microvasculature of the human vagina by NOS and neuropeptide- containing nerves. J Anat, 186: 633-644.
  • Hoshi A, Takahashi M, Fujii J, Myint T, Kaneto H, Suzuki K, Yamasaki Y, Kamada T, Taniguchi N. 1996. Glycation and inactivation of sorbitol dehydrogenase in normal and diabetic rats. Biochem J, 318: 119-123.
  • Ireland JJ, Murphee RL, Coulson PB. 1980. Accuracy of predicting stages of bovine estrous cycle by gross appearance of the corpus luteum. J Dairy Sci, 63: 155-160.
  • Jeffery J, Jornvall H. 1988. Sorbitol dehydrogenase. Advances in. Enzymol, 61: 47-106.
  • Johansson K, El-Ahmad M, Kaiser C, Jornvall H, Eklund H, Hoog, JO, 2001. Crystal structure of sorbitol dehydrogenase. Chem Biol Interact, 130: 351-358.
  • Kador PF, Kinoshita JH, Stribling D, Brittain DR, Mirrless DJ, Sennitt CM. 1987. Rat lens aldose reductase and poliol production. Biochem J, 247:495-496.
  • Kocna P, Fric P, Zavoral M, Pelech T. 1996. Arginase activity determination. A marker of large bowel mucosal proliferation. Eur J Clin Biochem, 34: 619–623.
  • Latonelle K, Le Menn F, Kaushik S, J, Pelissero C, B, 2002. Effects of dietary phytoestrogens in vivo and in vitro in rainbow trout and siberian sturgeon: interests and limits of the in vitro studies of interspecies differences. General and Comparative Endocrinology, 126: 39-51.
  • Nishimura C, Matsuura Y, Kokai Y, Akera T, Carper D, Morjana, N. 1990. Cloning and expression of human aldose reductase. J Biol Chem, 265: 9788-9792.
  • Razmi N, Jelodar GA, Nazifi S, Dehghani A. 2005. Arginase status in cattle reproductive system. Vet Arhiv, 75:31-38.
  • Razmi N, Jelodar GA, Nazifi S, Dehghani A. 2005. Arginase status in cattle reproductive system. Vet Arhiv, 75: 31-38.
  • Reiersen H, Lindstad, RI, Mckinley-Mckee, JS. 1994. The inactivation of sheep liver sorbitol dehydrogenase by pyrophosphate and some analogous metal chelators. Biochem Biophys, 311: 450-456.
  • Takahashi M, Fujii J, Teshima T, Suzuki K, Shiba T, Taniguchi N. 1993. Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression. Gene, 127: 249-253.
  • Tanimoto T, Maekawa K, Okada S, Yabe Nishimura C. 1998. Clinical analysis of aldose reductase for differential diagnosis of the pathogenesis of diabetic complication. Analytica Chimica Acta, 365: 285-292.
  • Underwood, EJ, Stuttle, NF. 1999. The mineral nutrition of livestock. Selenium. CAB International Wallingford, UK, 421- 474.
  • Wermuth B, Munch, JD and Von Wartburg, JP. 1977. Purification and properties of NADPH-dependent aldehyde reductase from human liver. JBC, 252:3821–3828.
  • Wilson L. 2003. Arginase inhibitors touted as potential drug target for sexual dysfunction. Biochem, 81: 9.
  • Yallampalli C, Dongy YL. 2000. Estradiol-17 inhibits nitric oxide synthase (NOS)-II and stimulates NOS-III gene expression in the rat uterus. Biol Reprod, 63:34-41.
  • Yu H, Yoo PK, Aguirre CC, Tsoa RW, Kern RM, Grody WW. 2003. Widespread expression of arginase I in mouse tissues: Biochemical and physiological implications. J Histoch Cytoch, 51: 1151–1160.
  • Yüksel M, Kandemir FM, Deveci H, Özdemir N. 2012. İneklerde seksüel siklusun farklı dönemlerinde uterus arginaz seviyelerinin araştırılması. YYÜ Vet Fak Derg 23(1): 15-17.
Toplam 34 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Konular Ziraat Mühendisliği
Bölüm Reviews
Yazarlar

Neslihan Güven 0000-0002-3344-4017

Ömer Kaya 0000-0001-6313-4848

Ercan Soydan 0000-0003-1634-4046

Yayımlanma Tarihi 1 Ekim 2019
Gönderilme Tarihi 18 Nisan 2019
Kabul Tarihi 23 Eylül 2019
Yayımlandığı Sayı Yıl 2019 Cilt: 2 Sayı: 4

Kaynak Göster

APA Güven, N., Kaya, Ö., & Soydan, E. (2019). The Enzymes That Affect the Reproduction in Certain Farm Animals. Black Sea Journal of Agriculture, 2(4), 224-229.

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