scholarly journals Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii

2004 ◽  
Vol 271 (15) ◽  
pp. 3115-3126 ◽  
Author(s):  
Alan P. Maloney ◽  
Susan M. Callan ◽  
Patrick G. Murray ◽  
Maria G. Tuohy
Keyword(s):  
Malate Dehydrogenase ◽  
Filamentous Fungus ◽  
Talaromyces Emersonii ◽  
Mitochondrial Malate Dehydrogenase

Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase

Biochemistry ◽  
1987 ◽  
Vol 26 (1) ◽  
pp. 128-134 ◽  
Author(s):  
Paula M. Grant ◽  
Steven L. Roderick ◽  
Gregory A. Grant ◽  
Leonard J. Banaszak ◽  
Arnold W. Strauss
Keyword(s):  
Malate Dehydrogenase ◽  
Rat Heart ◽  
Mitochondrial Malate Dehydrogenase

Mitochondrial Malate Dehydrogenase of Bovine Cerebrum

1975 ◽  
Vol 78 (5) ◽  
pp. 989-999 ◽  
Author(s):  
Haruhiro HIGASHIDA ◽  
Ritsuko K. SEMBA ◽  
Fujiko NIWA ◽  
Shigeo KASHIWAMATA
Keyword(s):  
Malate Dehydrogenase ◽  
Mitochondrial Malate Dehydrogenase

scholarly journals MALATE DEHYDROGENASE ISOZYMES OF THE CHICK EMBRYO

1965 ◽  
Vol 13 (6) ◽  
pp. 510-514 ◽  
Author(s):  
JAMES L. CONKLIN ◽  
EDWARD J. NEBEL
Keyword(s):  
Lactate Dehydrogenase ◽  
Chick Embryo ◽  
Malate Dehydrogenase ◽  
Molecular Basis ◽  
Specific Pattern ◽  
Starch Gel Electrophoresis ◽  
Organ Specific ◽  
Malate Dehydrogenase Isozymes ◽  
Starch Gel ◽  
Mitochondrial Malate Dehydrogenase

Malate dehydrogenase fractions of the chick embryo were demonstrated after starch gel electrophoresis of homogenates of liver, brain and spleen. A total of seven malate dehydrogenase fractions were observed to occur in the chick embryo in an organ specific pattern. Treatment of the homogenates with urea, sodium chloride-sodium phosphate, and p-chloromercuribenzoate prior to electrophoresis revealed that only three distinct malate dehydrogenase-active proteins were presence. Two of these proteins exhibited properties similar to those previously reported for the supernatant malate dehydrogenase and mitochondrial malate dehydrogenase of other species. Becuase of the differing properties of chick malate and lactate dehydrogenase it is concluded that the molecular basis for malate dehydrogenase isozymes is different from that reported for lactate dehydrogenase isozymes.

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