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Enzymes for Research, Diagnostic and Industrial Use

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Native Rabbit Pyruvate Kinase/Lactic Dehydrogenase enzymes

Cat No.
NATE-0568
Description
Lactate dehydrogenase from rabbit muscle can be inhibited by ascorbate. Aldolase and actin were shown to block this inhibitory effect. Pyruvate kinase requires bivalent and monovalent cations such as Mg2+ and K+ respectively for activation to occur.
Abbr
PK/LDH enzymes, Native (Rabbit)
Alias
PK/LDH enzymes
Source
rabbit muscle
Species
Rabbit
Applications
Pyruvate kinase from rabbit muscle has been used in a study to assess nuclear magnetic relaxation studies of the conformation of adenosine 5′-triphosphate. It has also been used in a study to investigate heterogeneity of presumably homogeneous protein preparations.
Product Overview
Pyruvate kinase from rabbit muscle catalyzes an ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate. buffered aqueous glycerol solution, 900-1400 units/mL lactic dehydrogenase, 600-1 kDa units/mL pyruvate kinase
Form
buffered aqueous glycerol solution
Activity
900-1400 units/mL lactic dehydrogenase; 600-1,000 units/mL pyruvate kinase
Unit Definition
Pyruvate kinase activity: One unit will convert 1.0 μmole of phospho (enol)pyruvate to pyruvate per min at pH 7.6 at 37°C. Lactic dehydrogenase activity: One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37°C.
Stability
−20°C
Buffer
Solution in 50% glycerol containing 10 mM HEPES, pH 7.0, 100 mM KCl and 0.1 mM EDTA
Synonyms
Pyruvate Kinase/Lactic Dehydrogenase enzymes; PK/LDH enzymes

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