Glucose-6-phosphate dehydrogenase Partial characterization of the rat liver and uterine enzymes

Terrence M. Donohue; Theodore A. Mahowald; David J. Adams; Kenneth L. Barker

doi:10.1016/0005-2744(81)90306-5

Glucose-6-phosphate dehydrogenase Partial characterization of the rat liver and uterine enzymes

Terrence M. Donohue, Theodore A. Mahowald, David J. Adams, Kenneth L. Barker

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

8 Scopus citations

Abstract

Some properties of rat liver and uterine glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP⁺ oxidoreductase, EC 1.1.1.49) have been determined. A procedure has been used for the purification of rat liver glucose-6-phosphate dehydrogenase to homogeneity (spec. act. 210-225 units/mg protein) from large amounts of liver (0.5-2 kg) with yields of up to 30%. Uterine glucose-6-phosphate dehydrogenase was obtained by immunoprecipitation methods and the properties of radioactively-labeled forms of this enzyme were then determined. The amino acid composition of the liver enzyme was found to be similar to that for the enzyme from other mammalian tissues. The liver and uterine enzymes have a subunit molecular weight of 57 000 and a pI of 6.5. The NH₂-terminal amino acid of both enzymes was found to be pyroglutamate.

Original language	English (US)
Pages (from-to)	356-368
Number of pages	13
Journal	BBA - Enzymology
Volume	658
Issue number	2
DOIs	https://doi.org/10.1016/0005-2744(81)90306-5
State	Published - Apr 14 1981

Keywords

(Uterus, Liver)
Amino-terminus
Glucose-6-phosphate dehydrogenase
Pyroglutamate

ASJC Scopus subject areas

Medicine(all)

Access to Document

10.1016/0005-2744(81)90306-5

Cite this

@article{ce17542b314b4bb18fe06972c46eee94,

title = "Glucose-6-phosphate dehydrogenase Partial characterization of the rat liver and uterine enzymes",

abstract = "Some properties of rat liver and uterine glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP+ oxidoreductase, EC 1.1.1.49) have been determined. A procedure has been used for the purification of rat liver glucose-6-phosphate dehydrogenase to homogeneity (spec. act. 210-225 units/mg protein) from large amounts of liver (0.5-2 kg) with yields of up to 30%. Uterine glucose-6-phosphate dehydrogenase was obtained by immunoprecipitation methods and the properties of radioactively-labeled forms of this enzyme were then determined. The amino acid composition of the liver enzyme was found to be similar to that for the enzyme from other mammalian tissues. The liver and uterine enzymes have a subunit molecular weight of 57 000 and a pI of 6.5. The NH2-terminal amino acid of both enzymes was found to be pyroglutamate.",

keywords = "(Uterus, Liver), Amino-terminus, Glucose-6-phosphate dehydrogenase, Pyroglutamate",

author = "Donohue, {Terrence M.} and Mahowald, {Theodore A.} and Adams, {David J.} and Barker, {Kenneth L.}",

year = "1981",

month = apr,

day = "14",

doi = "10.1016/0005-2744(81)90306-5",

language = "English (US)",

volume = "658",

pages = "356--368",

journal = "BBA - Enzymology",

issn = "0005-2744",

publisher = "Elsevier BV",

number = "2",

}

TY - JOUR

T1 - Glucose-6-phosphate dehydrogenase Partial characterization of the rat liver and uterine enzymes

AU - Donohue, Terrence M.

AU - Mahowald, Theodore A.

AU - Adams, David J.

AU - Barker, Kenneth L.

PY - 1981/4/14

Y1 - 1981/4/14

N2 - Some properties of rat liver and uterine glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP+ oxidoreductase, EC 1.1.1.49) have been determined. A procedure has been used for the purification of rat liver glucose-6-phosphate dehydrogenase to homogeneity (spec. act. 210-225 units/mg protein) from large amounts of liver (0.5-2 kg) with yields of up to 30%. Uterine glucose-6-phosphate dehydrogenase was obtained by immunoprecipitation methods and the properties of radioactively-labeled forms of this enzyme were then determined. The amino acid composition of the liver enzyme was found to be similar to that for the enzyme from other mammalian tissues. The liver and uterine enzymes have a subunit molecular weight of 57 000 and a pI of 6.5. The NH2-terminal amino acid of both enzymes was found to be pyroglutamate.

AB - Some properties of rat liver and uterine glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP+ oxidoreductase, EC 1.1.1.49) have been determined. A procedure has been used for the purification of rat liver glucose-6-phosphate dehydrogenase to homogeneity (spec. act. 210-225 units/mg protein) from large amounts of liver (0.5-2 kg) with yields of up to 30%. Uterine glucose-6-phosphate dehydrogenase was obtained by immunoprecipitation methods and the properties of radioactively-labeled forms of this enzyme were then determined. The amino acid composition of the liver enzyme was found to be similar to that for the enzyme from other mammalian tissues. The liver and uterine enzymes have a subunit molecular weight of 57 000 and a pI of 6.5. The NH2-terminal amino acid of both enzymes was found to be pyroglutamate.

KW - (Uterus, Liver)

KW - Amino-terminus

KW - Glucose-6-phosphate dehydrogenase

KW - Pyroglutamate

UR - http://www.scopus.com/inward/record.url?scp=0019879678&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019879678&partnerID=8YFLogxK

U2 - 10.1016/0005-2744(81)90306-5

DO - 10.1016/0005-2744(81)90306-5

M3 - Article

C2 - 7248306

AN - SCOPUS:0019879678

SN - 0005-2744

VL - 658

SP - 356

EP - 368

JO - BBA - Enzymology

JF - BBA - Enzymology

IS - 2

ER -

Glucose-6-phosphate dehydrogenase Partial characterization of the rat liver and uterine enzymes

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this