The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin

Mark Pines; Peter Gierschik; Allen Spiegel

doi:10.1016/0014-5793(85)80332-X

The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin

Mark Pines, Peter Gierschik, Allen Spiegel

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

8 Scopus citations

Abstract

The 35-kDa β-subunit of transducin purified from rod outer segment membranes is cleaved into 2 major fragments by trypsin, and 7 major fragments by chymotrypsin. Identical fragments are visualized by immunoblotting with transducin-β specific antisera after proteolysis of rod outer segment membranes, purified brain guanine nucleotide binding proteins, and brain membranes. The results indicate that the β-subunits of transducin and of brain guanine nucleotide binding proteins are not only similar structurally, but are also similarly oriented in membranes with respect to accessibility to proteolytic enzymes.

Original language	English (US)
Pages (from-to)	355-359
Number of pages	5
Journal	FEBS Letters
Volume	182
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(85)80332-X
State	Published - Mar 25 1985
Externally published	Yes

Keywords

Adenylate cyclase
Guanine nucleotide binding protein
Photoreceptor
Transmembrane signalling

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(85)80332-X

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@article{d458182180e249078831348ad5d1a76c,

title = "The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin",

abstract = "The 35-kDa β-subunit of transducin purified from rod outer segment membranes is cleaved into 2 major fragments by trypsin, and 7 major fragments by chymotrypsin. Identical fragments are visualized by immunoblotting with transducin-β specific antisera after proteolysis of rod outer segment membranes, purified brain guanine nucleotide binding proteins, and brain membranes. The results indicate that the β-subunits of transducin and of brain guanine nucleotide binding proteins are not only similar structurally, but are also similarly oriented in membranes with respect to accessibility to proteolytic enzymes.",

keywords = "Adenylate cyclase, Guanine nucleotide binding protein, Photoreceptor, Transmembrane signalling",

author = "Mark Pines and Peter Gierschik and Allen Spiegel",

note = "Funding Information: We are gratefult o C. Woodard and R. Vinitzky for expertt echnicala ssistancea, nd to G. Milligan and W. Klee for providing purified brain G pro- teins.M .P. is on sabbaticalle avef rom the Volcani Agricultural ResearchC enter, Rehovoth, Israel. P.G. wass upportedin part by a grant( Gi 138/1-l) from the DeutscheF orschungsgemeinschaft.",

year = "1985",

month = mar,

day = "25",

doi = "10.1016/0014-5793(85)80332-X",

language = "English (US)",

volume = "182",

pages = "355--359",

journal = "FEBS Letters",

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number = "2",

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T1 - The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin

AU - Pines, Mark

AU - Gierschik, Peter

AU - Spiegel, Allen

N1 - Funding Information: We are gratefult o C. Woodard and R. Vinitzky for expertt echnicala ssistancea, nd to G. Milligan and W. Klee for providing purified brain G pro- teins.M .P. is on sabbaticalle avef rom the Volcani Agricultural ResearchC enter, Rehovoth, Israel. P.G. wass upportedin part by a grant( Gi 138/1-l) from the DeutscheF orschungsgemeinschaft.

PY - 1985/3/25

Y1 - 1985/3/25

N2 - The 35-kDa β-subunit of transducin purified from rod outer segment membranes is cleaved into 2 major fragments by trypsin, and 7 major fragments by chymotrypsin. Identical fragments are visualized by immunoblotting with transducin-β specific antisera after proteolysis of rod outer segment membranes, purified brain guanine nucleotide binding proteins, and brain membranes. The results indicate that the β-subunits of transducin and of brain guanine nucleotide binding proteins are not only similar structurally, but are also similarly oriented in membranes with respect to accessibility to proteolytic enzymes.

AB - The 35-kDa β-subunit of transducin purified from rod outer segment membranes is cleaved into 2 major fragments by trypsin, and 7 major fragments by chymotrypsin. Identical fragments are visualized by immunoblotting with transducin-β specific antisera after proteolysis of rod outer segment membranes, purified brain guanine nucleotide binding proteins, and brain membranes. The results indicate that the β-subunits of transducin and of brain guanine nucleotide binding proteins are not only similar structurally, but are also similarly oriented in membranes with respect to accessibility to proteolytic enzymes.

KW - Adenylate cyclase

KW - Guanine nucleotide binding protein

KW - Photoreceptor

KW - Transmembrane signalling

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U2 - 10.1016/0014-5793(85)80332-X

DO - 10.1016/0014-5793(85)80332-X

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C2 - 3920073

AN - SCOPUS:0021821814

SN - 0014-5793

VL - 182

SP - 355

EP - 359

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin

Abstract

Keywords

ASJC Scopus subject areas

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