Study on bull sperm lactate dehydrogenase.
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Animals↗
Biomedical subjects
G H Georgiev
Publications and source records attributed to G H Georgiev.
A study of bovine acrosomal proteins.
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Acrosome↗
Isoelectric focusing of bull seminal plasma proteins.
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Animals↗
Disc electrophoresis of LDH in bull seminal plasma.
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Animals↗
Comparative studies on the activity and polymorphism of enzymes in the semen of farm animals and birds--I. Electrophoretic investigation into the non-specific esterases in bull seminal plasma.
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Animals↗
Activity of sorbitol dehydrogenase in ram's and bull's seminal plasma.
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Alcohol Oxidoreductases↗
A study on the anaerobic metabolism in the semen of bulls of different breeds.
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Anaerobiosis↗
On the polymorphism of the acid phosphatase in bull's and ram's semenal plasma.
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Acid Phosphatase↗
Sorbitol dehydrogenase activity in spermatozoa of the domestic fowl, Gallus domesticus.
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Alcohol Oxidoreductases↗
Electrophoretic study of bull sperm acrosin.
The electrophoretic study was carried out on acrosin isozymes in crude acetic acid bovine acrosomal material. The separation of isozymes was performed by means of cathodic disc electrophoretic system. The four major isozymes were established in most of the studied sperm samples. In some cases were found variations in the zymographic pattern-increasing or reduction in the number of isozymes.
Acrosin↗
Electrophoresis of NADH-dependent oxidoreductase (diaphorase) in boar spermatozoa.
Two forms of NADH-dependent oxidoreductase (diaphorase [EC.1.6.99.-]) are established in boar spermatozoa. The first form is typical for soluble proteins with a varying electrophoretic profile, while the other form for sedimental proteins with a specific, slowly-moving fraction, which is not common for the soluble form. The two enzyme forms have a close isoelectric point (pI5.5-6.0) and they can not be inhibited by dicumarol 10(-5) mol l-1 and FAD 10(-4) mol l-1. The molecular mass of the soluble form of the enzyme is 28, 37, 46 and 67 kD, while of the sedimental form it is 220, 250 and 260 kD, respectively.
Animals↗