Amino acid sequence of dogfish muscle lactate dehydrogenase.
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چکیده
منابع مشابه
Amino acid sequence of dogfish muscle lactate dehydrogenase.
Lactate dehydrogenase isolated from vertebrate tissues catalyzes the reversible oxidation of L-lactic acid to pyruvic acid. The catalysis requires nicotinamide adenine dinucleotide (NAD’) as a coenzyme and is specific for the A-hydrogen of the nicotinamide ring (1) (Fig. 1). Although the enzyme is tetrameric, no cooperative effects have been observed between subunits (2). Each identical subunit...
متن کاملThe amino acid sequence of the tryptic peptides isolated from dogfish M4 lactate dehydrogenase.
The peptides which result from treatment of the S-[14C]carboxymethyl derivative of dogfish M4 lactate dehydrogenase (EC 1.1.1.27) with trypsin have been isolated and their sequences have been elucidated. Each identical subunit has a molecular weight of 36,000 and on the basis of the amino acid composition 40 unique tryptic peptides are anticipated. Thirty-seven of these peptides have been isola...
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A number of reports have appeared in recent years on the mechanism, i.e. the mode of enzyme and substrate interaction, of anaerobic dehydrogenases. For example, the mechanisms of heart muscle lactate dehydrogenase (1)) yeast alcohol dehydrogenase (2), and ribitol dehydrogenase (3) appear to involve a compulsory sequence of enzyme and substrate interaction leading to one or more kinetically impo...
متن کاملCharacterization of rabbit lactate dehydrogenase-M and lactate dehydrogenase-H cDNAs. Control of lactate dehydrogenase expression in rabbit muscle.
Two cDNA clones were isolated, one corresponding to the mRNA coding for lactate dehydrogenase-M (LDH-M), the other to the mRNA coding for lactate dehydrogenase-H (LDH-H). The cDNA inserts consist of the entire open reading frame for LDH-M and a partial sequence, from amino acid 117 to 332, for LDH-H. Using these two clones as probes we demonstrate that: (a) the abundance of mRNA is muscle-type ...
متن کاملAmino acid sequence of a fragment of rabbit muscle aldolase.
Cleavage of rabbit muscle aldolase by cyanogen bromide results in the formation of four fragments of different size [1]. Study of the primary structure of the enzyme has been based on the examination of these fragments [1, 2]. Because of the insolubility and associated problems due to the relatively large size of the fragments Lai [1], as well as Anderson et al. [3], used pyridine-acetic acid b...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)40621-1