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Isolation and characterization of a high molecular weight glycoprotein from human blood platelets.

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Lawler, J.W., Slayter, H.S., Coligan, J.E.·1978·Journal of Biological Chemistry

Abstract

A high molecular weight glycoprotein consisting of three disulfide-linked 142,000 molecular weight chains has been isolated from human blood platelets. The glycoprotein, designated thrombospondin, is released by platelets in response to thrombin treatment and is proteolyzed when left in the presence of platelets after liberation. It is relatively insensitive to degradation by thrombin. Thrombospondin is a filamentous protein of dimensions approximately 7 X 70 nm and contains 1.9% neutral sugars, 1.4% amino sugars, 0.7% sialic acid, and no hexuronic acid. Amino acid analysis reveals that the level of cysteine is approximately 260 residues per molecule. Thrombospondin binds to immobilized heparin but is released by 0.45 M sodium chloride. A single band is obtained by isoelectric focusing, indicating a pI of 4.7 as well as a relatively high degree of purity. Degradation of the intact molecule with trypsin yields a stable core particle of molecular weight 210,000 comprised of three 70,000 chains.

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Metadata

Authors
Lawler, J. W., Slayter, H. S., & Coligan, J. E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1978-12
Volume
253
Issue
23
Pages
8609-8616
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1505957065
Cited by
433
References
0
FWCI
5.64
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Isolation and characterization of a high molecular weight glycoprotein from human blood platelets. https://app.cochat.ai/papers/10.1016/s0021-9258(17)34336-3
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Lawler, J. W., Slayter, H. S., & Coligan, J. E. (1978). Isolation and characterization of a high molecular weight glycoprotein from human blood platelets. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)34336-3

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