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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
01/08/1992 |
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Data da última atualização: |
07/08/2023 |
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Autoria: |
BILASPURI, G. S.; DEOL, K. K. |
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Título: |
Biochemical studies on acid phosphatase in the goat (Capra hircus) testis. |
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Ano de publicação: |
1983 |
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Fonte/Imprenta: |
Zentralblatt für Veterinärmedizin. Reihe A, v. 30, n. 7, p. 498-505, 1983. |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: A biochemical study was made to characterize the Acph in the total testicular homogenate of the adult goat (Capra hircus) as well as the different enzymes revealed by acrylamide gel electrophoresis. Total Acph activity was doubled by a two-fold increase in enzyme concentration. A hyperbolic curve of Acph was found with an increase in substrate concentration. V,,and Km values were, respectively, 7.5 uM of p-nitrophenol released/min./mg protein and 2 mM. pH optima were pH 5 (acetate buffer) and pH 4.5 (citrate phosphate buffer). The optimal temperature was 30 oC. The divalent metal ions activated Acph in the decreasing order of Mnz+, Co'+, Mg2+ and Zn2+. Cuz+, NaF and DDVP decreased enzyme activity gradually with increasing concentrations. Formaldehyde and acetone completely inhibited Acph activity, while triton x-100 had no effect. Acrylamide gel electrophoresis of total homogenate with a-naphthyl phosphate revealed three enzymes (I, 11 and 111) of acid phosphatase which varied in their biochemical characteristics. Enzyme I was the most thermo-resistant; at 70 "C the activity of all three enzymes ceased. Metal ions (Mn2+, Mg", Co2+, Znz+), especially Mnz+, markedly activated enzyme III; enzyme I was only slightly activated, and enzyme I1 remained unaffected. Copper (4 mM) markedly inhibited all enzymes. NaF (500 pM) eliminated the activity of enzyme 11 and that of enzymes I and 111 was also markedly decreased. It is concluded, as in other mammalian species studied to date, multiple forms of acid phosphatases exist in the testis of the goat. MenosAbstract: A biochemical study was made to characterize the Acph in the total testicular homogenate of the adult goat (Capra hircus) as well as the different enzymes revealed by acrylamide gel electrophoresis. Total Acph activity was doubled by a two-fold increase in enzyme concentration. A hyperbolic curve of Acph was found with an increase in substrate concentration. V,,and Km values were, respectively, 7.5 uM of p-nitrophenol released/min./mg protein and 2 mM. pH optima were pH 5 (acetate buffer) and pH 4.5 (citrate phosphate buffer). The optimal temperature was 30 oC. The divalent metal ions activated Acph in the decreasing order of Mnz+, Co'+, Mg2+ and Zn2+. Cuz+, NaF and DDVP decreased enzyme activity gradually with increasing concentrations. Formaldehyde and acetone completely inhibited Acph activity, while triton x-100 had no effect. Acrylamide gel electrophoresis of total homogenate with a-naphthyl phosphate revealed three enzymes (I, 11 and 111) of acid phosphatase which varied in their biochemical characteristics. Enzyme I was the most thermo-resistant; at 70 "C the activity of all three enzymes ceased. Metal ions (Mn2+, Mg", Co2+, Znz+), especially Mnz+, markedly activated enzyme III; enzyme I was only slightly activated, and enzyme I1 remained unaffected. Copper (4 mM) markedly inhibited all enzymes. NaF (500 pM) eliminated the activity of enzyme 11 and that of enzymes I and 111 was also markedly decreased. It is concluded, as in other mammalian species studied t... Mostrar Tudo |
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Palavras-Chave: |
Andrologia; Hydrogen-Ion Concentration; Isoenzymes. |
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Thesagro: |
Caprino; Fosfatase Ácida; Reprodução; Testículo. |
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Thesaurus Nal: |
Acid phosphatase; Enzymology; Goats; Males; Reproduction; Testes. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02369naa a2200289 a 4500
001 1521751
005 2023-08-07
008 1983 bl uuuu u00u1 u #d
100 1 $aBILASPURI, G. S.
245 $aBiochemical studies on acid phosphatase in the goat (Capra hircus) testis.$h[electronic resource]
260 $c1983
520 $aAbstract: A biochemical study was made to characterize the Acph in the total testicular homogenate of the adult goat (Capra hircus) as well as the different enzymes revealed by acrylamide gel electrophoresis. Total Acph activity was doubled by a two-fold increase in enzyme concentration. A hyperbolic curve of Acph was found with an increase in substrate concentration. V,,and Km values were, respectively, 7.5 uM of p-nitrophenol released/min./mg protein and 2 mM. pH optima were pH 5 (acetate buffer) and pH 4.5 (citrate phosphate buffer). The optimal temperature was 30 oC. The divalent metal ions activated Acph in the decreasing order of Mnz+, Co'+, Mg2+ and Zn2+. Cuz+, NaF and DDVP decreased enzyme activity gradually with increasing concentrations. Formaldehyde and acetone completely inhibited Acph activity, while triton x-100 had no effect. Acrylamide gel electrophoresis of total homogenate with a-naphthyl phosphate revealed three enzymes (I, 11 and 111) of acid phosphatase which varied in their biochemical characteristics. Enzyme I was the most thermo-resistant; at 70 "C the activity of all three enzymes ceased. Metal ions (Mn2+, Mg", Co2+, Znz+), especially Mnz+, markedly activated enzyme III; enzyme I was only slightly activated, and enzyme I1 remained unaffected. Copper (4 mM) markedly inhibited all enzymes. NaF (500 pM) eliminated the activity of enzyme 11 and that of enzymes I and 111 was also markedly decreased. It is concluded, as in other mammalian species studied to date, multiple forms of acid phosphatases exist in the testis of the goat.
650 $aAcid phosphatase
650 $aEnzymology
650 $aGoats
650 $aMales
650 $aReproduction
650 $aTestes
650 $aCaprino
650 $aFosfatase Ácida
650 $aReprodução
650 $aTestículo
653 $aAndrologia
653 $aHydrogen-Ion Concentration
653 $aIsoenzymes
700 1 $aDEOL, K. K.
773 $tZentralblatt für Veterinärmedizin. Reihe A$gv. 30, n. 7, p. 498-505, 1983.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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