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Author Resmi, K. R. ♦ Krishnan, L. K.
Source Sree Chitra Tirunal Institute for Medical Sciences & Technology
Content type Text
Publisher Thrombosis Research
File Format PDF
Language English
Subject Domain (in DDC) Technology ♦ Medicine & health ♦ Diseases
Subject Domain (in MeSH) Hemic and Immune Systems ♦ Anatomy
Subject Keyword Hematology
Abstract beta-thromboglobulin (beta-TG) is a platelet-specific protein present in the alpha-granules and secreted into the surrounding medium on cell activation. The sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of platelet releasate after inhibition of metalloproteinases with ethyleneglycol-bis-(beta-aminoethyl ether) N,N'-tetra acetic acid (EGTA) showed disappearance of an 8.0-kDa band. In the absence of the cation chelators, a 48-kDa band disappeared and concurrently, the 8.0-kDa band intensity increased suggesting that the former may be the immediate precursor of the latter. The Western blot stained using specific antibodies, isolated from single-cell clones of hybridoma, against 8.0 kDa protein recognized not only 48 and 8.0 kDa bands but few others too. The data suggests that one or more high molecular weight protein is released from alpha-granules and is broken down into smaller fragments after release to form beta-thromboglobulin (beta-TG)-like proteins by the action of metal dependent proteases. (C) 2002 Elsevier Science Ltd. All rights reserved.
Education Level UG and PG
Learning Resource Type Article
Educational Framework Medical Council of India (MCI)
Volume Number 106
Issue Number 41004
Page Count 8
Starting Page 229
Ending Page 236