By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Sulfur Amino Acids have been published. According to news reporting originating from New Delhi, India, by NewsRx correspondents, research stated, "The cystatins form a superfamily of structurally related proteins with highly conserved structural folds. They are all potent, reversible, competitive inhibitors of cysteine proteinases (CPs)."
Our news editors obtained a quote from the research from the All India Institute of Medical Sciences, "Proteins from this group present differences in proteinase inhibition despite their high level of structural similarities. In this study, three cysteine proteinase inhibitors (CPIs) of low molecular weight were isolated from human seminal fluid (HSF) by affinity chromatography on carboxymethyl (CM)-papain Sepharose column, purified using various chromatographic procedures and checked for purity on sodium-dodecyl PAGE (SDS-PAGE). Matrix-assisted laser desorption-ionization-time-of flight-mass spectrometry (MALDI-TO-FMS) identified these proteins as cystatin 9, cystatin SN, and SAP-1 (an N-terminal truncated form of cystatin S). All three CPIs suppressed the activity of papain potentially and showed remarkable heat stability. Interestingly SAP-1 also inhibits the activity of trypsin, chymotrypsin, pepsin, and PSA (prostate specific antigen) and acts as a cross-class protease inhibitor in in vitro studies. Using Surface Plasmon Resonance, we have also observed that SAP-1 shows a significant binding with all these proteases. These studies suggest that SAP-1 is a cross-class inhibitor that may regulate activity of various classes of proteases within the reproductive systems."
According to the news editors, the research concluded: "To our knowledge, this is the first report about purification of CPIs from HSF; the identification of such proteins could provide better insights into the physiological processes and offer intimation for further research."
For more information on this research see: Three low molecular weight cysteine proteinase inhibitors of human seminal fluid: Purification and enzyme kinetic properties. Biochimie, 2013;95(8):1552-1559. Biochimie can be contacted at: Elsevier France-Editions Scientifiques Medicales Elsevier, 23 Rue Linois, 75724 Paris, France. (Elsevier - www.elsevier.com; Biochimie - www.elsevier.com/wps/product/cws_home/505803)
The news editors report that additional information may be obtained by contacting V.K. Yadav, All India Inst Med Sci, Dept. of Lab Med, New Delhi 110029, India. Additional authors for this research include N. Chhikara, K. Gill, S. Dey, S. Singh and S. Yadav (see also Sulfur Amino Acids).
Keywords for this news article include: Asia, India, Cysteine, Peptides, New Delhi, Cystatins, Proteinase, Sulfur Amino Acids, Neutral Amino Acids, Sulfhydryl Compounds, Enzymes and Coenzymes
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