Reduced Nicotinamide-adenine Dinucleotide and Pyruvate in Urea-denaturation of Lactic Dehydrogenase Isozymes

Nature ◽  
1966 ◽  
Vol 209 (5018) ◽  
pp. 79-80 ◽  
Author(s):  
SEPPO LINDY ◽  
AARNE KONTTINEN
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Lactic Dehydrogenase ◽  
Nicotinamide Adenine ◽  
Urea Denaturation ◽  
Reduced Nicotinamide Adenine Dinucleotide

A Continuous Spectrophotometric Method for the Determination of Leucine Aminopeptidase

1968 ◽  
Vol 14 (6) ◽  
pp. 555-564 ◽  
Author(s):  
J A Knight ◽  
D T Hunter
Keyword(s):  
Spectrophotometric Method ◽  
Nicotinamide Adenine Dinucleotide ◽  
Leucine Aminopeptidase ◽  
Lactic Dehydrogenase ◽  
New Method ◽  
Nicotinamide Adenine ◽  
Glutamic Pyruvic Transaminase ◽  
Peptide Hydrolase ◽  
Reduced Nicotinamide Adenine Dinucleotide

Abstract A new method to assay the enzyme, leucine aminopeptidase (LAP; L-leucyl-peptide hydrolase—3.4.1.1), is described. The technic is an extension of the conventional glutamic-pyruvic transaminase (GPT) reaction. Serum LAP is allowed to react with the substrate L-leucyl-L-alanine to quantitatively generate alanine. This alanine, in the presence of excess α-ketoglutaric acid and GPT, rapidly forms pyruvate, which is converted to lactate by excess lactic dehydrogenase (LDH). Reduced nicotinamide adenine dinucleotide (NAD) is quantitatively oxidized in this reaction. The change in reduced NAD concentration is followed by continuous spectrophotometry at 340 mµ.

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