The binding of folyl polyglutamates by hemoglobin

Reinhold Benesch; Samuel Waxman; Ruth Benesch; Charles Baugh

doi:10.1016/0006-291X(82)91263-3

The binding of folyl polyglutamates by hemoglobin

Reinhold Benesch
, Samuel Waxman
, Ruth Benesch
, Charles Baugh

Icahn School of Medicine at Mount Sinai

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

11 Scopus citations

Abstract

Pteroyl polyglutamates bind to hemoglobin with an affinity which leaves only a minor fraction of red cell folate in the free state. This could serve as a regulating mechanism for protein synthesis in the differentiating erythroblast.

Original language	English
Pages (from-to)	1359-1363
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	106
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(82)91263-3
State	Published - 30 Jun 1982

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title = "The binding of folyl polyglutamates by hemoglobin",

abstract = "Pteroyl polyglutamates bind to hemoglobin with an affinity which leaves only a minor fraction of red cell folate in the free state. This could serve as a regulating mechanism for protein synthesis in the differentiating erythroblast.",

author = "Reinhold Benesch and Samuel Waxman and Ruth Benesch and Charles Baugh",

note = "Funding Information: ACKNOWLEDGEMENTS Research supported by National ROl-AM-16690, National Science Chemotherapy Foundation.",

year = "1982",

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day = "30",

doi = "10.1016/0006-291X(82)91263-3",

language = "English",

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T1 - The binding of folyl polyglutamates by hemoglobin

AU - Benesch, Reinhold

AU - Waxman, Samuel

AU - Benesch, Ruth

AU - Baugh, Charles

N1 - Funding Information: ACKNOWLEDGEMENTS Research supported by National ROl-AM-16690, National Science Chemotherapy Foundation.

PY - 1982/6/30

Y1 - 1982/6/30

N2 - Pteroyl polyglutamates bind to hemoglobin with an affinity which leaves only a minor fraction of red cell folate in the free state. This could serve as a regulating mechanism for protein synthesis in the differentiating erythroblast.

AB - Pteroyl polyglutamates bind to hemoglobin with an affinity which leaves only a minor fraction of red cell folate in the free state. This could serve as a regulating mechanism for protein synthesis in the differentiating erythroblast.

UR - https://www.scopus.com/pages/publications/0020464834

U2 - 10.1016/0006-291X(82)91263-3

DO - 10.1016/0006-291X(82)91263-3

M3 - Article

C2 - 6180751

AN - SCOPUS:0020464834

SN - 0006-291X

VL - 106

SP - 1359

EP - 1363

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

The binding of folyl polyglutamates by hemoglobin

Abstract

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