Amylase in Human Semen

Povoa, H

doi:10.1016/s0022-5347(17)64540-3

Cited by 15 publications

(9 citation statements)

References 5 publications

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“…The present study was also in agreement with the observation of Provoa [15] and Moon and Bunge [1], i.e. significant changes in the activity of seminal a-amylase amongst the normo-, oligo-, and azoospermie group.…”

Section: Discussionsupporting

confidence: 93%

Enzymic Activities in the Seminal Plasma of Normospermie, Oligospermie and Infertile Azoospermie Men

Sk¹,

Bhattacharyya²

1984

Enzyme

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Section: Discussionsupporting

confidence: 93%

Enzymic Activities in the Seminal Plasma of Normospermie, Oligospermie and Infertile Azoospermie Men

Sk¹,

Bhattacharyya²

1984

Enzyme

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“…Crabo et al (1971) suggest the use of GOT measurement as an indication of fertility of the semen. This possibility is found also in the work of several other authors (Pumpianski and Sharon, 1965;Povoa, 1964;Joel and Herzberg, 1965;and Roussel and Stallcup, 1965) which indicate a significant relationship between GOT enzyme activity and sperm concentration. Brown et al (1972) believe, however, that for a measure of fertility after freezing, a more meaningful criterion for the assay of cell damage would be the persistence of motility.…”

Section: Introductionsupporting

confidence: 68%

Enzymes and Electrolytes in the Semen of Japanese Quail

Buxton

Orcutt

1975

Poultry Science

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Japanese quail (Coturnix coturnix japonica) semen was collected at 10 a.m., 2 p.m., or 6 p.m. for four consecutive days during four consecutive weeks. All but the first day's collections were analyzed for sodium, potassium, chloride, carbon dioxide, H+ concentration, cell count, volume and total sperm number. A random sample was then collected for the analysis of amylase and another random sample was collected for the analysis of glutamic oxalacetic transaminase (GOT), creatine phosphokinase (CPK), and lactic dehydrogenase (LDH). The activities of GOT and LDH in quail semen were approximately ten times higher than those obtained for larger fowl (chickens and turkeys) and mammals. While CPK levels have not been measured in other animals, its activity in quail semen is probably also high. There was a significant difference between the enzyme activity of the sperm and seminal plasma for GOT and CPK. The parameters of sodium, potassium, chloride, carbon dioxide, H+ concentration, cell count, volume, and total sperm number did not show a significant variation at the hours of 10 a.m., 2 p.m., and 6 p.m. Three of these parameters (cell count, potassium, and chloride), however did show significant variation during collection over three consecutive days, the chloride decreasing and potassium and cell count first decreasing and then by the third day returning to levels of the first day. None of the parameters followed the sperm concentration closely enough to be of value as an index of quail fertility.

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“…On the other hand, human spermatozoa contained mainly an aspartate aminotransferase isoenzyme with cationic properties and only a trace of the anionic form. This may indicate that the observed correlation between aspartate aminotransferase activity and sperm density in human semen (Povoa & Villela, 1960;Povoa, 1964;Joel 8c Herzberg, 1965) may not entirely be due to a leakage of the enzyme from the spermatozoa. This indication is further supported by the observation that no change in transaminase activity occurred in whole semen or seminal plasma with time.…”

Section: Discussionmentioning

confidence: 96%

Transaminase in Human Semen

Eliasson¹

1967

Reproduction

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Determinations of aspartate and alanine aminotransferase activity in human semen were carried out by the spectrophotometric and colorimetric methods. It was found that the occurrence of interfering substances in semen makes the spectrophotometric method unsuitable without prior partial purification of the enzyme. The mean activity determined colorimetrically in 417 samples of human semen was 320 Sigma-Frankel units/ml (s.e.m. \m=+-\8,range 10 to 1070) for aspartate aminotransferase and 30 units/ml (s.e.m. \ m=+-\ 3, range 0 to 97, n = 40) for alanine aminotransferase. As regards aspartate aminotransferase, the activity of this enzyme was highest at +60\s=deg\ C. Pyridoxal phosphate increased the activity, particularly if added to semen samples with initially low activity. Gel electrophoresis of seminal plasma showed one band migrating towards the anode. However, in homogenized spermatozoa the bulk of enzyme migrated towards the cathode and only a weak band could be demonstrated on the side of the anode.

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Amylase in Human Semen

Cited by 15 publications

References 5 publications

Enzymic Activities in the Seminal Plasma of Normospermie, Oligospermie and Infertile Azoospermie Men

Enzymic Activities in the Seminal Plasma of Normospermie, Oligospermie and Infertile Azoospermie Men

Enzymes and Electrolytes in the Semen of Japanese Quail

Transaminase in Human Semen

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