Properties of hepatic hexose-6-phosphate dehydrogenase purified from brook trout and lake trout

John J. Stegeman; Erwin Goldberg

doi:10.1016/0305-0491(72)90282-9

Properties of hepatic hexose-6-phosphate dehydrogenase purified from brook trout and lake trout

John J. Stegeman^*, Erwin Goldberg

^*Corresponding author for this work

Molecular Biosciences

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

15 Scopus citations

Abstract

1. 1. Brook trout hexose-6-phosphate dehydrogenase (H6PD) and lake trout H6PD are essentially identical in several parameters including pH optima, kinetic properties and activation energy. They differ in thermal stability. 2. 2. The various oxidations catalyzed by trout H6PD differ in their response to the presence of Mg²⁺, ATP and several anions. 3. 3. The apparent K_m's of all four substrates show a decrease with decreasing temperature. 4. 4. Kinetics of substrate oxidation by H6PD suggest that the enzyme most likely functions as a G6PD.

Original language	English (US)
Pages (from-to)	241-256
Number of pages	16
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	43
Issue number	2
DOIs	https://doi.org/10.1016/0305-0491(72)90282-9
State	Published - Oct 15 1972

Keywords

ATP
Glucose-6-phosphate dehydrogenase
Mg
Salvelinus fontinalis
Salvelinus namaycush
acclimation
activation energy
anions
brook trout
enzyme inhibition
enzyme kinetics
enzyme stimulation
hexose-6-phosphate dehydrogenase
isoelectric point
lake trout
pH optima
salmonids
thermal denaturation

ASJC Scopus subject areas

Biochemistry
Physiology
Molecular Biology

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10.1016/0305-0491(72)90282-9

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title = "Properties of hepatic hexose-6-phosphate dehydrogenase purified from brook trout and lake trout",

abstract = "1. 1. Brook trout hexose-6-phosphate dehydrogenase (H6PD) and lake trout H6PD are essentially identical in several parameters including pH optima, kinetic properties and activation energy. They differ in thermal stability. 2. 2. The various oxidations catalyzed by trout H6PD differ in their response to the presence of Mg2+, ATP and several anions. 3. 3. The apparent Km's of all four substrates show a decrease with decreasing temperature. 4. 4. Kinetics of substrate oxidation by H6PD suggest that the enzyme most likely functions as a G6PD.",

keywords = "ATP, Glucose-6-phosphate dehydrogenase, Mg, Salvelinus fontinalis, Salvelinus namaycush, acclimation, activation energy, anions, brook trout, enzyme inhibition, enzyme kinetics, enzyme stimulation, hexose-6-phosphate dehydrogenase, isoelectric point, lake trout, pH optima, salmonids, thermal denaturation",

author = "Stegeman, {John J.} and Erwin Goldberg",

note = "Funding Information: Acknowledgements--We are grateful to J. P. Cuerrier and J. C. Ward, Canadian Wildlife Service, for generously providing fish used in this investigation. The research was supported in part by National Science Foundation Grant GB-7271 and by United States Public Health Service Predoctoral Fellowship 4 F01 GM41704-03.",

year = "1972",

month = oct,

day = "15",

doi = "10.1016/0305-0491(72)90282-9",

language = "English (US)",

volume = "43",

pages = "241--256",

journal = "Comparative Biochemistry and Physiology -- Part B: Biochemistry and",

issn = "0305-0491",

publisher = "Elsevier Inc.",

number = "2",

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TY - JOUR

T1 - Properties of hepatic hexose-6-phosphate dehydrogenase purified from brook trout and lake trout

AU - Stegeman, John J.

AU - Goldberg, Erwin

N1 - Funding Information: Acknowledgements--We are grateful to J. P. Cuerrier and J. C. Ward, Canadian Wildlife Service, for generously providing fish used in this investigation. The research was supported in part by National Science Foundation Grant GB-7271 and by United States Public Health Service Predoctoral Fellowship 4 F01 GM41704-03.

PY - 1972/10/15

Y1 - 1972/10/15

N2 - 1. 1. Brook trout hexose-6-phosphate dehydrogenase (H6PD) and lake trout H6PD are essentially identical in several parameters including pH optima, kinetic properties and activation energy. They differ in thermal stability. 2. 2. The various oxidations catalyzed by trout H6PD differ in their response to the presence of Mg2+, ATP and several anions. 3. 3. The apparent Km's of all four substrates show a decrease with decreasing temperature. 4. 4. Kinetics of substrate oxidation by H6PD suggest that the enzyme most likely functions as a G6PD.

AB - 1. 1. Brook trout hexose-6-phosphate dehydrogenase (H6PD) and lake trout H6PD are essentially identical in several parameters including pH optima, kinetic properties and activation energy. They differ in thermal stability. 2. 2. The various oxidations catalyzed by trout H6PD differ in their response to the presence of Mg2+, ATP and several anions. 3. 3. The apparent Km's of all four substrates show a decrease with decreasing temperature. 4. 4. Kinetics of substrate oxidation by H6PD suggest that the enzyme most likely functions as a G6PD.

KW - ATP

KW - Glucose-6-phosphate dehydrogenase

KW - Mg

KW - Salvelinus fontinalis

KW - Salvelinus namaycush

KW - acclimation

KW - activation energy

KW - anions

KW - brook trout

KW - enzyme inhibition

KW - enzyme kinetics

KW - enzyme stimulation

KW - hexose-6-phosphate dehydrogenase

KW - isoelectric point

KW - lake trout

KW - pH optima

KW - salmonids

KW - thermal denaturation

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U2 - 10.1016/0305-0491(72)90282-9

DO - 10.1016/0305-0491(72)90282-9

M3 - Article

C2 - 4144724

AN - SCOPUS:0015510983

SN - 0305-0491

VL - 43

SP - 241

EP - 256

JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

IS - 2

ER -

Properties of hepatic hexose-6-phosphate dehydrogenase purified from brook trout and lake trout

Abstract

Keywords

ASJC Scopus subject areas

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