Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Changes of aldolase A and B protein levels and their mRNA levels due to starvation for 48 h in mucosae of the jejunum, ileum, and colon were determined by Western and Northern blot analyses. In fed rats, B protein and B mRNA were predominant in the jejunum. In the ileum, both A protein and A mRNA, as much as B protein and B mRNA, were present in significant amounts. In the colon, A protein and A mRNA were predominant. The enzyme activity levels in those segments of fed rat intestine were in parallel to total enzyme protein levels (A + B) and also to total mRNA levels (A + B), thus suggesting that aldolase isozyme expression in fed rat intestine is determined mainly at the level of transcription. Starvation for 48 h caused about 30% reduction of both B protein level and B mRNA level in jejunum. In the ileum, both A and B mRNA levels were lowered 30-40% from those of fed rats, while A and B protein levels were reduced slightly (A, 0%; B, 12%). In the colon, starvation caused about 50% increase of A mRNA level and about 10% reduction of A protein level. By measuring the synthetic rate of the enzyme proteins from in vivo [35S]methionine incorporation, the accumulation of A mRNA in this tissue was suggested to be due to the significant fall of the translation rate of A mRNA. The translational and post-translational controls of aldolase isozyme expressions in rat intestines are discussed.
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PMID:Dietary regulation of aldolase isozyme expression in rat intestinal mucosa. 357 91

Amidination of aldolase, glyceraldehyde-3-phosphate dehydrogenase, tryptophan synthetase B protein, L-arabinose isomerase, and the catalytic subunit of E. coli aspartate transcarbamylase with the bifunctional reagent dimethyl suberimidate produces cross-linked proteins, with reaction predominating within oligomers. Disc electrophoresis of a modified protein on polyacrylamide gel in the presence of sodium dodecyl sulfate resolves a set of species with molecular weights equal to integral multiples of the protomer molecular weight. For oligomers composed of identical protomers, the number of principal species observed is identical to the number of protomers in the oligomer. Application of the method to two proteins composed of dissimilar protomers, native aspartate transcarbamylase and tryptophan synthetase alpha(2)beta(2) complex of E. coli, revealed differences in the reactivities of the different kinds of protomer within each oligomer.
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PMID:Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins. 491 6