Association of a GDP binding activity with initiation factor eIF-2 from calf liver

Evan A. Stringer; Asok Chaudhuri; Umadas Maitra

doi:10.1016/0006-291X(77)90764-1

Association of a GDP binding activity with initiation factor eIF-2 from calf liver

Evan A. Stringer, Asok Chaudhuri, Umadas Maitra

Developmental & Molecular Biology

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

8 Scopus citations

Abstract

A highly purified preparation of the eucaryotic initiation factor eIF-2 from calf liver which forms a ternary complex with GTP and Met-tRNA_f^Met also exhibits a potent GDP binding activity. The factor preparation specifically forms a binary complex with GDP, other ribonucleoside diphosphates and GTP are inactive. Evidence is presented indicating that the GTP-dependent Met-tRNA_f^Met binding and binary complex formation with GDP are mediated by the same protein which has an apparent molecular weight of 67,000 as judged by glycerol density gradient centrifugation.

Original language	English (US)
Pages (from-to)	586-592
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	76
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(77)90764-1
State	Published - May 23 1977

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/0006-291X(77)90764-1

Fingerprint Dive into the research topics of 'Association of a GDP binding activity with initiation factor eIF-2 from calf liver'. Together they form a unique fingerprint.

Cite this

@article{095418c42cb447c4afb5293c1b6a9ec6,

title = "Association of a GDP binding activity with initiation factor eIF-2 from calf liver",

abstract = "A highly purified preparation of the eucaryotic initiation factor eIF-2 from calf liver which forms a ternary complex with GTP and Met-tRNAfMet also exhibits a potent GDP binding activity. The factor preparation specifically forms a binary complex with GDP, other ribonucleoside diphosphates and GTP are inactive. Evidence is presented indicating that the GTP-dependent Met-tRNAfMet binding and binary complex formation with GDP are mediated by the same protein which has an apparent molecular weight of 67,000 as judged by glycerol density gradient centrifugation.",

author = "Stringer, {Evan A.} and Asok Chaudhuri and Umadas Maitra",

note = "Funding Information: ACKNOWLEDGEMENTS: This work was supported by grants stitutes of Health and the American Cancer Society. Research Awardee of the American Cancer Society.",

year = "1977",

month = may,

day = "23",

doi = "10.1016/0006-291X(77)90764-1",

language = "English (US)",

volume = "76",

pages = "586--592",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Association of a GDP binding activity with initiation factor eIF-2 from calf liver

AU - Stringer, Evan A.

AU - Chaudhuri, Asok

AU - Maitra, Umadas

N1 - Funding Information: ACKNOWLEDGEMENTS: This work was supported by grants stitutes of Health and the American Cancer Society. Research Awardee of the American Cancer Society.

PY - 1977/5/23

Y1 - 1977/5/23

N2 - A highly purified preparation of the eucaryotic initiation factor eIF-2 from calf liver which forms a ternary complex with GTP and Met-tRNAfMet also exhibits a potent GDP binding activity. The factor preparation specifically forms a binary complex with GDP, other ribonucleoside diphosphates and GTP are inactive. Evidence is presented indicating that the GTP-dependent Met-tRNAfMet binding and binary complex formation with GDP are mediated by the same protein which has an apparent molecular weight of 67,000 as judged by glycerol density gradient centrifugation.

AB - A highly purified preparation of the eucaryotic initiation factor eIF-2 from calf liver which forms a ternary complex with GTP and Met-tRNAfMet also exhibits a potent GDP binding activity. The factor preparation specifically forms a binary complex with GDP, other ribonucleoside diphosphates and GTP are inactive. Evidence is presented indicating that the GTP-dependent Met-tRNAfMet binding and binary complex formation with GDP are mediated by the same protein which has an apparent molecular weight of 67,000 as judged by glycerol density gradient centrifugation.

UR - http://www.scopus.com/inward/record.url?scp=0017393018&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017393018&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(77)90764-1

DO - 10.1016/0006-291X(77)90764-1

M3 - Article

C2 - 1036137

AN - SCOPUS:0017393018

VL - 76

SP - 586

EP - 592

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

Association of a GDP binding activity with initiation factor eIF-2 from calf liver

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this