Kinetics of lactate dehydrogenase from heart and white muscle of ocean pout: a single isozyme system

1986 ◽  
Vol 64 (12) ◽  
pp. 2665-2668 ◽  
Author(s):  
John M. Stewart ◽  
William R. Driedzic
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Kinetic Properties ◽  
Lactate Oxidase ◽  
Dehydrogenase Isozyme ◽  
Lactate Dehydrogenase Isozyme ◽  
Kinetics Of ◽  
Insight Into ◽  
Dominant Direction

Heart and white skeletal muscle of ocean pout (Macrozoarces americanus) express only a single lactate dehydrogenase isozyme based on electrophoretic and immunological analysis. The enzyme has been partially purified and its kinetic properties elucidated in both the pyruvate reductase and lactate oxidase directions. Km values and responses to changing pH catagorize the enzyme as a classical skeletal muscle type lactate dehydrogenase. The kinetic parameters are assessed with respect to known in situ carbon flux rates through this locus. It is concluded that the enzyme data per se provide little insight into either the dominant direction or the net maximal rate of carbon flow.

scholarly journals THE DISTRIBUTION OF LACTATE DEHYDROGENASE ISOZYMES IN HUMAN SKELETAL MUSCLE FIBERS

1964 ◽  
Vol 12 (8) ◽  
pp. 608-614 ◽  
Author(s):  
M. VAN WIJHE ◽  
M. C. BLANCHAER ◽  
S. ST. GEORGE-STUBBS
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Human Skeletal Muscle ◽  
Muscle Fibers ◽  
Isozyme Pattern ◽  
Electrophoretic Separation ◽  
Lactate Dehydrogenase Isozymes ◽  
Dehydrogenase Isozyme ◽  
Lactate Dehydrogenase Isozyme ◽  
Normal Human

A study of the distribution of lactate dehydrogenase isozymes in single fibers from normal human skeletal muscle is presented. The fibers were classified into red, intermediate and white types on histochemical grounds and their lactate dehydrogenase isozyme content assessed by electrophoretic separation in veronal buffered agar. The results generally agreed with previous homogenate studies on animal skeletal muscle, in that the white fibers contained almost exclusively isozymes IV and V, whereas red fibers were rich in isozymes I, II and III, but IV and V also appeared indigenous to these fibers. The intermediate fibers had an isozyme pattern combining the features of red and white fibers. The metabolic implications of these findings are discussed.

Skeletal muscle lactate dehydrogenase isozyme alterations in men and women marathon runners

1986 ◽  
Vol 61 (2) ◽  
pp. 477-481 ◽  
Author(s):  
F. S. Apple ◽  
M. A. Rogers
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Fiber Type ◽  
Muscle Lactate ◽  
Marathon Runners ◽  
Men And Women ◽  
Type Composition ◽  
Before And After ◽  
Dehydrogenase Isozyme ◽  
Lactate Dehydrogenase Isozyme

Total lactate dehydrogenase (LD) and LD isozyme activities in gastrocnemius muscle from trained men and women runners were measured in response to the chronic stress of training for a marathon race (42.2 km). Following 9 wk of training, total LD activity in skeletal muscle from men and women runners significantly (P less than 0.02) decreased 2.26 and 2.25 U/mg protein, respectively. However, men's total LD activities were significantly (P less than 0.001) less than the women's both before and after training. Significant (P less than 0.05) increases in LD1 activities in skeletal muscle in men and women runners were also observed after training. No significant correlations were detected between percent fiber type composition in men or women vs. the changes in total LD activity, changes in LD1 activity, maximal O2 consumption or training distance averaged per week after the training period. The biochemical adaptations in skeletal muscle that occurred in the LD isozyme composition in both men and women runners make the runners skeletal muscle appear similar to heart muscle in LD1 and LD2 activities.

scholarly journals DEVELOPMENTAL CHANGE AND REGIONAL DIFFERENCE OF THE LACTATE DEHYDROGENASE ISOZYME PATTERN IN RAT BRAIN

1980 ◽  
Vol 13 (2) ◽  
pp. 164-172
Author(s):  
KANKATSU YUN ◽  
TAKESHI MATSUO ◽  
TAKASHI ORIBE ◽  
TSUTOMU TOMIOKA ◽  
TAKAYOSHI IKEDA
Keyword(s):  
Lactate Dehydrogenase ◽  
Rat Brain ◽  
Regional Difference ◽  
Developmental Change ◽  
Isozyme Pattern ◽  
Dehydrogenase Isozyme ◽  
Lactate Dehydrogenase Isozyme

Kinetics of Thyroid Hormone Induced Changes in Liver and Skeletal Muscle Enzymes of Clarias batrachus

1999 ◽  
Vol 54 (5-6) ◽  
pp. 458-462 ◽  
Author(s):  
G. Tripathi
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Metabolic Enzymes ◽  
Time Dependent ◽  
Clarias Batrachus ◽  
Muscle Enzymes ◽  
Induced Changes ◽  
Kinetics Of ◽  
Mitochondrial Malate Dehydrogenase

Abstract Kinetics of triiodothyronine (T3) induced changes were studied in cytoplasmic malate dehydrogenase (cMDH), mitochondrial malate dehydrogenase (mMDH) and lactate dehydrogenase (LDH) of the liver and skeletal muscle of a catfish, Clarias batrachus. The rates of gradual inductions in the activities of all the three metabolic enzymes were faster in skeletal muscle than those of the liver. These time-dependent and tissue-specific inductions may be due to the possible differences in the rates of different enzymic syntheses. The maximum inductions in the activities of cMDH, mMDH and LDH were recorded around 19 hr after T3 treatment. Thereafter, the activities of all the enzymes gradually declined to their half levels within the next 12 hr which reflected the physiological half-life of these metabolic enzymes in the freshwater catfish.

Hepatitis B "e" antigen: an apparent association with lactate dehydrogenase isozyme-5

Science ◽  
1977 ◽  
Vol 198 (4321) ◽  
pp. 1068-1070 ◽  
Author(s):  
G. Vyas ◽  
D. Peterson ◽  
R. Townsend ◽  
Damle ◽  
L. Magnius
Keyword(s):  
Lactate Dehydrogenase ◽  
Hepatitis B ◽  
Hepatitis B E Antigen ◽  
Dehydrogenase Isozyme ◽  
Lactate Dehydrogenase Isozyme ◽  
Apparent Association
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