Kinetic evidence for enhanced regulatory capacity of malate dehydrogenase due to formation of enzyme-membrane complexes

被引：0

|

作者：

Gainullin, M ^{[1
]}

Khvatova, E ^{[1
]}

机构：

[1] Med Acad, Nizhnii Novgorod, Russia

来源：

JOURNAL OF NEUROCHEMISTRY | 2001年 / 78卷

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D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

引用

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页码：159 / 159

页数：1

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[1] Kinetic evidence for protein complexes between thioredoxin and NADP-malate dehydrogenase and presence of a thioredoxin binding site at the N-terminus of the enzyme
Braun, H
Lichter, A
Haberlein, I
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 240 (03): : 781 - 788
[2] Kinetic evidence for protein complexes between thioredoxin and NADP-malate dehydrogenase and presence of a thioredoxin binding site at the N-terminus of the enzyme
Eur J Biochem, 3 (781):
[3] FORMATION OF P-COUMARIC ACID AND O-COUMARIC ACID FROM L-PHENYLALANINE BY MICROSOMAL MEMBRANE-FRACTIONS FROM POTATO - EVIDENCE OF MEMBRANE-BOUND ENZYME COMPLEXES
CZICHI, U
KINDL, H
PLANTA, 1975, 125 (02) : 115 - 125
[4] KINETIC STUDIES ON BACTERIAL PLASMA-MEMBRANE ATPASE (F1) - NUCLEOTIDE-INDUCED LONG-TERM INACTIVATION OF ATP HYDROLYZING ACTIVITY IS LINKED TO FORMATION OF MULTIPLE TIGHT ENZYME NUCLEOTIDE COMPLEXES
HOCKEL, M
HULLA, FW
RISI, S
DOSE, K
JOURNAL OF BIOLOGICAL CHEMISTRY, 1978, 253 (12) : 4292 - 4296