Incorporation of carbohydrate into protein of human platelets

Philip D. Zieve; Morton Schmukler

doi:10.1016/0304-4165(74)90089-0

Incorporation of carbohydrate into protein of human platelets

Philip D. Zieve, Morton Schmukler

School of Medicine

Research output: Contribution to journal › Article › peer-review

Abstract

Human platelets incorporated glucosamine and mannose into protein. Incorporation in whole or disrupted cells was reduced considerably by incubation with thrombin. The effect of thrombin appeared to be due to hydrolysis of glycoprotein. Cyanide and fluoride also markedly inhibited incorporation; concanavalin A, prostaglandin E₁, aspirin, ADP, and puromycin had no effect. Neither concanavalin A, ADP or prostaglandin E₁ blocked the inhibition of incorporation by thrombin. The experiments indicate that human platelets add carbohydrate onto pre-existing protein by an energy-dependent process and that this glycoprotein is hydrolyzed by thrombin.

Original language	English (US)
Pages (from-to)	225-229
Number of pages	5
Journal	BBA - General Subjects
Volume	372
Issue number	1
DOIs	https://doi.org/10.1016/0304-4165(74)90089-0
State	Published - Nov 4 1974

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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title = "Incorporation of carbohydrate into protein of human platelets",

abstract = "Human platelets incorporated glucosamine and mannose into protein. Incorporation in whole or disrupted cells was reduced considerably by incubation with thrombin. The effect of thrombin appeared to be due to hydrolysis of glycoprotein. Cyanide and fluoride also markedly inhibited incorporation; concanavalin A, prostaglandin E1, aspirin, ADP, and puromycin had no effect. Neither concanavalin A, ADP or prostaglandin E1 blocked the inhibition of incorporation by thrombin. The experiments indicate that human platelets add carbohydrate onto pre-existing protein by an energy-dependent process and that this glycoprotein is hydrolyzed by thrombin.",

author = "Zieve, {Philip D.} and Morton Schmukler",

note = "Funding Information: Supported by a grant HL-09102 from the National Heart Institute and an Institutional Research Grant, 5--90-IRR0556-10, to Baltimore City Hospitals. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

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N2 - Human platelets incorporated glucosamine and mannose into protein. Incorporation in whole or disrupted cells was reduced considerably by incubation with thrombin. The effect of thrombin appeared to be due to hydrolysis of glycoprotein. Cyanide and fluoride also markedly inhibited incorporation; concanavalin A, prostaglandin E1, aspirin, ADP, and puromycin had no effect. Neither concanavalin A, ADP or prostaglandin E1 blocked the inhibition of incorporation by thrombin. The experiments indicate that human platelets add carbohydrate onto pre-existing protein by an energy-dependent process and that this glycoprotein is hydrolyzed by thrombin.

AB - Human platelets incorporated glucosamine and mannose into protein. Incorporation in whole or disrupted cells was reduced considerably by incubation with thrombin. The effect of thrombin appeared to be due to hydrolysis of glycoprotein. Cyanide and fluoride also markedly inhibited incorporation; concanavalin A, prostaglandin E1, aspirin, ADP, and puromycin had no effect. Neither concanavalin A, ADP or prostaglandin E1 blocked the inhibition of incorporation by thrombin. The experiments indicate that human platelets add carbohydrate onto pre-existing protein by an energy-dependent process and that this glycoprotein is hydrolyzed by thrombin.

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Incorporation of carbohydrate into protein of human platelets

Abstract

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