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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1976-1-23
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pubmed:abstractText |
1. Pig M4 lactate dehydrogenase treated in the dark with pyridoxal 5'-phosphate at pH8.5 and 25 degrees C loses activity gradually. The maximum inactivation was 66%, and this did not increase with concentrations of pyridoxal 5'-phosphate above 1 mM. 2. Inactivation may be reversed by dialysis or made permanent by reducing the enzyme with NaBH4. 3. Spectral evidence indicates modification of lysine residues, and 6-N-pyridoxyl-lysine is present in the hydrolsate of inactivated, reduced enzyme. 4. A second cycle of treatment with pyridoxal 5'-phosphate and NaBH4 further decreases activity. After three cycles only 9% of the original activity remains. 5. Apparent Km values for lactate and NAD+ are unaltered in the partially inactivated enzyme. 6. These results suggest that the covalently modified enzyme is inactive; failure to achieve complete inactivation in a single treatment is due to the reversibility of Schiff-base formation and to the consequent presence of active non-covalently bonded enzyme-modifier complex in the equilibrium mixture. 7. Although several lysine residues per subunit are modified, only one appears to be essential for activity: pyruvate and NAD+ together (both 5mM) completely protect against inactivation, and there is a one-to-one relationship between enzyme protection and decreased lysine modification. 8. NAD+ or NADH alone gives only partial protection. Substrates give virtually none. 9. Pig H4 lactate dehydrogenase is also inactivated by pyridoxal 5'-phosphate. 10. The possible role of the essential lysine residue is discussed.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-1126546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-1237292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-13376585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-13539037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-13654337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-13883267,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4147977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4193186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4291474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4295777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4301490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4309753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4319106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4326829,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-4795361,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-5655493,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1238085-5961876
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
149
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
107-13
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1238085-Animals,
pubmed-meshheading:1238085-Binding Sites,
pubmed-meshheading:1238085-Borohydrides,
pubmed-meshheading:1238085-Isoenzymes,
pubmed-meshheading:1238085-Kinetics,
pubmed-meshheading:1238085-L-Lactate Dehydrogenase,
pubmed-meshheading:1238085-Lysine,
pubmed-meshheading:1238085-Muscles,
pubmed-meshheading:1238085-Oxidation-Reduction,
pubmed-meshheading:1238085-Protein Binding,
pubmed-meshheading:1238085-Pyridoxal Phosphate,
pubmed-meshheading:1238085-Swine
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pubmed:year |
1975
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pubmed:articleTitle |
Modification of pig M4 lactate dehydrogenase by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue.
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pubmed:publicationType |
Journal Article
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