A less toxic heparin antagonist - low molecular weight protamine

J. F. Liang; L. Zhen; L. Chang; V. C. Yang

A less toxic heparin antagonist - low molecular weight protamine

J. F. Liang, L. Zhen, L. Chang, V. C. Yang

Department of Chemistry and Chemical Biology

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

9 Scopus citations

Abstract

A new thirteen amino acid peptide, named low molecular weight protamine (LMWP), was obtained through the enzymatic digestion of native protamine. Both in vitro and in vivo results showed that LMWP fully maintained the heparin neutralization function of protamine but had much lower immunogenicity and antigenicity. Unlike protamine, neither LMWP nor LMWP/heparin complexes caused significant blood platelet aggregation in rats. These results suggest that LMWP can be used as a substitute for protamine for developing a new generation of nontoxic heparin antagonists.

Original language	English
Pages (from-to)	139-144
Number of pages	6
Journal	Biokhimiya
Volume	68
Issue number	1
State	Published - 2003

Keywords

Heparin neutralization
Immunogenicity
Low molecular weight protamine
Platelet aggregation

Cite this

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title = "A less toxic heparin antagonist - low molecular weight protamine",

abstract = "A new thirteen amino acid peptide, named low molecular weight protamine (LMWP), was obtained through the enzymatic digestion of native protamine. Both in vitro and in vivo results showed that LMWP fully maintained the heparin neutralization function of protamine but had much lower immunogenicity and antigenicity. Unlike protamine, neither LMWP nor LMWP/heparin complexes caused significant blood platelet aggregation in rats. These results suggest that LMWP can be used as a substitute for protamine for developing a new generation of nontoxic heparin antagonists.",

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T1 - A less toxic heparin antagonist - low molecular weight protamine

AU - Liang, J. F.

AU - Zhen, L.

AU - Chang, L.

AU - Yang, V. C.

PY - 2003

Y1 - 2003

N2 - A new thirteen amino acid peptide, named low molecular weight protamine (LMWP), was obtained through the enzymatic digestion of native protamine. Both in vitro and in vivo results showed that LMWP fully maintained the heparin neutralization function of protamine but had much lower immunogenicity and antigenicity. Unlike protamine, neither LMWP nor LMWP/heparin complexes caused significant blood platelet aggregation in rats. These results suggest that LMWP can be used as a substitute for protamine for developing a new generation of nontoxic heparin antagonists.

AB - A new thirteen amino acid peptide, named low molecular weight protamine (LMWP), was obtained through the enzymatic digestion of native protamine. Both in vitro and in vivo results showed that LMWP fully maintained the heparin neutralization function of protamine but had much lower immunogenicity and antigenicity. Unlike protamine, neither LMWP nor LMWP/heparin complexes caused significant blood platelet aggregation in rats. These results suggest that LMWP can be used as a substitute for protamine for developing a new generation of nontoxic heparin antagonists.

KW - Heparin neutralization

KW - Immunogenicity

KW - Low molecular weight protamine

KW - Platelet aggregation

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M3 - Article

AN - SCOPUS:0037225827

SN - 0320-9725

VL - 68

SP - 139

EP - 144

JO - Biokhimiya

JF - Biokhimiya

IS - 1

ER -

A less toxic heparin antagonist - low molecular weight protamine

Abstract

Keywords

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