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R. ELIASSON

Summary.

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. ±8, range 10 to 1070) for aspartate aminotransferase and 30 units/ml (s.e.m. ±3, range 0 to 97, n = 40) for alanine aminotransferase. As regards aspartate aminotransferase, the activity of this enzyme was highest at +60° 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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R. ELIASSON

Summary.

The oxygen consumption of human spermatozoa has been determined polarographically with Clark electrodes both in whole semen and in a buffered Ringer solution. Washing of the spermatozoa caused an average decrease of 13% in the number of live cells. The oxygen consumption of the spermatozoa was two to three times higher in the Ringer solution than in the whole semen (P<0·001).

If the washed spermatozoa were returned to their own seminal plasma, the oxygen consumption also returned to the original level. These results indicated that human seminal plasma normally contains a factor that depresses sperm respiration.

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R. ELIASSON

Summary.

Human seminal plasma contains highly active glutamic oxaloacetic transaminase (aspartate aminotransferase). Using the splitejaculation method it has been demonstrated that the enzyme is largely concentrated in the first portion of the ejaculate, indicating that it is derived from the prostate gland.

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M. BYGDEMAN and R. ELIASSON

Summary.

Progesterone has an inhibitory action on the spontaneous motility and pharmacological reactivity of isolated myometrial strips from women in early pregnancy. This effect is similar to that observed on isolated uterine preparations from other species, such as rabbit, rat and mouse.

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S. Arver and R. Eliasson

Summary. Mean ± s.e.m. concentrations (nmol/108 cells) of zinc and magnesium in bull spermatozoa were 30·6 ± 6·6 and 119 ±28·8, respectively. Corresponding values for boar spermatozoa were 16·9 ± 1·98 and 57·1 ± 4·3. Bull spermatozoa washed twice in a standard buffered salt solution, pH 7·75, lost 72·6% of their zinc and 46·5% of their magnesium. Boar spermatozoa lost 40% of Zn and 18% of Mg, respectively. Addition of albumin (4% final concentration) to the washing solution did not increase the loss of ions from bull spermatozoa but increased the loss of zinc and magnesium from boar spermatozoa to 52% and 41%, respectively.

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J. SUOMINEN, R. ELIASSON and M. NIEMI

Summary.

Proteolytic activity, acid phosphatase activity and fructose concentration were measured in seminal plasma from 205 human semen samples. Certain routine sperm characteristics were also determined. High fibrinolytic activity was found and TAME-esterase and proteinase activity was also present in all specimens. The activity of all the proteolytic enzymes correlated positively with the acid phosphatase activity suggesting the prostate gland to be the origin of the enzymes. TAME-esterase activity was inversely related to the seminal fructose content. No correlation was observed between sperm characteristics and the seminal proteolytic enzymes. The specimens with abnormal viscosity usually contained low proteinase activity.