Two major, close molecular weight basic coagulum proteins of freshly ejaculated human semen identifiable on reducing SDS‐PAGE, have been isolated together from washed seminal coagulum. The latter was solubilized in urea, followed by reduction and carboxymethylation of disulphide bonds. By high‐resolution chromatography on carboxymethy‐Sephadex and Sephacryl S‐300 using 8 M urea in 0. 1m Tris‐HCl (pH 7.4) as eluate these proteins were isolated together (purity 99%) with a yield of 10.5%. The molecular weights of the isolated proteins on SDS‐PAGE were 75 and 79 kD. Copyright © 1994, Wiley Blackwell. All rights reserved

A MANDAL

A K BHATTACHARYYA

University of Calcutta (informally known as Calcutta University or CU) is a collegiate public state university located in Kolkata, West Bengal, India.&nbsp;Within India it is recognized as a &quot;Five-Star University&quot; and accredited &quot;A&quot; Grade by National Assessment and Accreditation Council.

&nbsp;

The University of Calcutta has secured the Fifth position among the Universities of India in the prestigious &quot;Indian University Ranking 2019&quot; list, released by the NIRF of the Ministry of Human Resource Development, Government of India.

&nbsp;

It was established on 24 January 1857, and was one of the first institutions in Asia to be established as a multidisciplinary and Western-style university. Its alumni and faculty include several heads of state, heads of government, social reformers, prominent artists, only academy award winner and Dirac medal winner in India, many Fellows of the Royal Society and five Nobel laureates as of 2019 which is highest in South Asia.

University Of Calcutta

International Journal of Andrology

This study demonstrated that semenogelin I and II, the predominant and the major basic human seminal coagulum proteins respectively were shown to be potent activators of sperm hyaluronidase. These proteins stimulated the activity of bovine testicular hyaluronidase, goat cauda sperm hyaluronidase and human ejaculated sperm hyaluronidase. Human seminal plasma protein, which predominantly contains the basic degradation residues of the basic coagulum proteins and albumin (pI 4.7) and which is also basic at the assay pH 3.8, also showed activation of bovine testicular hyaluronidase while acidic pepsin (pI < 1.0) exhibited no such activation. The findings may be utilized as an assay method for comparative evaluation of specific activation units of the purified basic seminal coagulum proteins or their cleavage products and for quantifying the total basic protein (pI > 3.8) units in human seminal plasma. One unit of the coagulum protein was defined as the amount of the activator that increases 1 mIU of hyaluronidase activity by 50%. The specific activity of the 57 kDa and 75-79 kDa coagulum proteins, and that of serum albumin against Sigma bovine testicular hyaluronidase (type IV), were 11 447, 8600 and 6252 units per mg protein respectively. It was speculated that human seminal coagulum proteins may have an activation effect on spermatozoal hyaluronidase activity in vivo. © 1995 Oxford University Press.

Human Reproduction

Andrology: Sperm hyaluronidase activation by purified predominant and major basic human seminal coagulum proteins

Summary. The predominant acidic coagulum protein of freshly ejaculated human semen under reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) was purified for the first time from washed seminal coagulum keeping urea throughout the entire procedure. Washed seminal coagulum was isolated from fresh semen sample in acetate buffer at pH 4.5 at 0 °C, solubilized rapidly in deionized 4 M urea followed by reduction and carboxymethylation of disulfide bonds. By CM‐Sephadex and Sephacryl S‐300 high‐ resolution chromatography in presence of urea at room temperature, the predominant acidic coagulum protein was highly purified (99.1 %) with a yield of 2.7% of the coagulum protein. The molecular weight of the purified protein in reducing SDS‐PAGE was 162 kD. 1994 Blackwell Verlag GmbH

Andrologia

First report on purification of the predominant acidic coagulum protein of human semen prior to liquefaction

Using SDS‐PAGE three major high molecular‐weight coagulum proteins (57, 75 and 79 kD) were identified in unliquefied human ejaculates. Washed coagulum was prepared at pH 4.5 and demonstrated negligible proteolysis as determined by a highly sensitive fluorescamine‐based method. Laser densitometric scanning of these high molecular‐weight proteins in unliquefied ejaculates in relation to their coagulational failure revealed that the total content of 57, 75 and 79 kD proteins in whole semen represented ˜ 44% of levels in the normally coagulated, ˜ 24% in poorly coagulated (P<0.005) and ˜ 3% in the non‐coagulated (alkaline liquid, P<0.001) samples. The findings imply that these predominant high molecular‐weight proteins play a major role in human seminal coagulum formation. Copyright © 1992, Wiley Blackwell. All rights reserved

Deficiency in major high molecularâ€weight seminal proteins in men producing poorly coagulating and alkaline liquid ejaculates

Intra-individual inter-ejaculate variations in the amounts of protein, fructose, N-acetylamino sugar, phosphate, sialic acid and amino sugar in washed coagulum from normal ejaculates of men were highly consistent (N = 9). All the prostatic components studied (acid phosphatase, zinc, calcium and citric acid), except zinc, in the washed coagulum were reduced by 90% of their values in semen (N = 5). The seminal vesicular markers (fructose, N-acetylamino sugar and phosphate) had no association with the coagulum structure and represented the soluble components (N = 5). The concentrations of protein and zinc in the coagulum were higher than those of semen by 114% and 32% respectively. The coagulum contained sialic acid and amino sugar as integrated components.

Journal	International Journal of Andrology
Publisher	-
ISSN	0105-6263