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https://www.ias.ac.in/article/fulltext/jbsc/033/02/0195-0207

Kallikrein; prostate cancer biomarker; proteinase activity; seminal plasma; tumour proliferation and metastasis; therapeutic target

Human seminal proteinase and prostate-specific antigen (PSA) were each isolated from human seminal fluid and compared. Both are glycoproteins of 32–34 kDa with protease activities. Based on some physicochemical, enzymatic and immunological properties, it is concluded that these proteins are in fact identical. The protein exhibits properties similar to kallikrein-like serine protease, trypsin, chymotrypsin and thiol acid protease. Tests of the activity of the enzyme against some potential natural and synthetic substrates showed that bovine serum albumin was more readily hydrolysed than casein. The results of this study should be useful in purifying and assaying this protein. Based on published studies and the present results, the broad proteolytic specificity of human seminal proteinase suggests a role for this protein in several physiological functions.

Abdul Waheed¹ Md Imtaiyaz Hassan² Robert L Van Etten³ Faizan Ahmad²

1. Edward A Doisy Department of Biochemistry and Molecular Biology, St Louis University School of Medicine, St Louis, MO 63104, USA
2. Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110 025, India
3. Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA

Manuscript received

3 November 2007

Accepted

26 February 2008

Early published

2 April 2008