Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1980-7-12
|
pubmed:abstractText |
The nutritional properties of protein bound epsilon-pyridoxyllysine residues in a phosphopyridoxyl bovine serum albumin (PP-BSA) preparation were examined by rat bioassay employing various levels of PP-BSA and pyridoxine (PN) fortification in the diets. Previous studies have shown that vitamin B-6 aldehydes can reductively bind to food proteins as epsilon-pyridoxyllysine complexes during processing and storage. The bound pyridoxyllysine was found to possess 50% molar vitamin B-6 activity, as indicated by slope ratios for rat growth, feed efficiency and liver pyridoxal 5'-phosphate concentration. The response curves indicated that high dosages of epsilon-pyridoxyllysine would fully satisfy the vitamin B-6 requirement. Direct antivitamin B-6 activity of epsilon-pyridoxyllysine was observed in diets containing low levels of PP-BSA. Classical rat acrodynia symptoms, depression of erythrocyte aspartate aminotransferase (AspAT) activity and elevation of in vitro coenzyme stimulation of AspAT were observed to be inversely related to PP-BSA concentration in the diet. The antivitamin B-6 effects were readily prevented by the presence of added 0.5--1.0 micrograms pyridoxing/g diet. In contrast to the previous study, the presence of PP-BSA in the diet did not inhibit the utilization of added PN. This difference was postulated to be due to a difference in vitamin B-6 concentration of the basal diets. The results of this study indicate that protein bound epsilon-pyridoxyllysine is nutritionally significant, presumably by its participation in the normal metabolism of vitamin B-6. The metabolic implications are discussed.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartate Aminotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Dietary Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxal,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxal Phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxine,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/epsilon-pyridoxyllysine,
http://linkedlifedata.com/resource/pubmed/chemical/pyridoxine 5-phosphate
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0022-3166
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
110
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
995-1005
|
pubmed:dateRevised |
2003-11-14
|
pubmed:meshHeading |
pubmed-meshheading:6768860-Animals,
pubmed-meshheading:6768860-Aspartate Aminotransferases,
pubmed-meshheading:6768860-Biological Assay,
pubmed-meshheading:6768860-Body Weight,
pubmed-meshheading:6768860-Dietary Proteins,
pubmed-meshheading:6768860-Dose-Response Relationship, Drug,
pubmed-meshheading:6768860-Erythrocytes,
pubmed-meshheading:6768860-Liver,
pubmed-meshheading:6768860-Lysine,
pubmed-meshheading:6768860-Male,
pubmed-meshheading:6768860-Protein Binding,
pubmed-meshheading:6768860-Pyridoxal,
pubmed-meshheading:6768860-Pyridoxal Phosphate,
pubmed-meshheading:6768860-Pyridoxine,
pubmed-meshheading:6768860-Rats,
pubmed-meshheading:6768860-Serum Albumin, Bovine
|
pubmed:year |
1980
|
pubmed:articleTitle |
Effects of epsilon-pyridoxyllysine bound to dietary protein on the vitamin B-6 status of rats.
|
pubmed:publicationType |
Journal Article
|