Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:4.1.2.13 (
aldolase
)
3,461
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The turnover of
3-methylhistidine
(N tau-methylhistidine) and in some cases actin, myosin heavy chain and
aldolase
in skeletal muscle was measured in a number of experiments in growing and adult rats in the fed and overnight-starved states. In growing fed rats in three separate experiments, measurements of the methylation rate of protein-bound
3-methylhistidine
by either [14C]- or [3H]-methyl-labelled S-adenosylmethionine show that
3-methylhistidine
synthesis is slower than the overall rate of protein synthesis indicated by [14C]tyrosine incorporation. Values ranged from 36 to 51%. However, in one experiment with rapidly growing young fed rats, acute measurements over 1 h showed that
3-methylhistidine
synthesis could be increased to the same rate as the overall rate. After overnight starvation in these rats, the steady-state synthesis rate of
3-methylhistidine
was 38.8% of the overall rate. This was a similar value to that in adult non-growing rats, in which measurements of the relative labelling of
3-methylhistidine
and histidine after a single injection of [14C]histidine indicated that
3-methylhistidine
synthesis was 37% of the overall rate in the fed or overnight-starved state. According to measurements of actin, myosin heavy-chain and
aldolase
synthesis in the over-night-starved state with young rats, with a variety of precursors, slow turnover of
3-methylhistidine
results from the specific slow turnover of actin, since turnover rates of myosin heavy chain, mixed protein and
aldolase
were 2.5, 3 and 3.4 times faster respectively. However, in the fed state synthesis rates of actin were increased disproportionately to give similar rates for all proteins. These results show that (a)
3-methylhistidine
turnover in muscle is less than half the overall rate in both young and adult rats, (b) slow
3-methylhistidine
turnover reflects the specifically slow turnover of actin compared with myosin heavy chain and other muscle proteins, and (c) during growth the synthesis rate of actin is particularly sensitive to the nutritional state and can be increased to a similar rate to that of other proteins.
...
PMID:Myofibrillar protein turnover. Synthesis of protein-bound 3-methylhistidine, actin, myosin heavy chain and aldolase in rat skeletal muscle in the fed and starved states. 661 82
Some experimental and clinical studies were done from the metabolic viewpoint to elucidate the characteristics of myonephropathic-metabolic syndrome. In experimental dogs with their femoral arteries ligated and two third of femoral muscles divided,
aldolase
and myoglobin showed remarkable increase without significant changes in electrolytes. Slight increase of GPT and GOT was observed. Amino acids showed elevation in urea, taurin, leucin, isoleucin, valine, threonine,
3-methylhistidine
, phenylalanine, histidine, lysine, methionine, tyrosine and anserin and decrease in glutamine, alanine, glycine, proline, carnosine, citrullin and arginine. In patients with acute arterial occlusion, potassium, GOT, LDH, CPK, lactate and pyruvate increased moderately and myoglobin showed remarkable increase and
aldolase
slight increase. Amino acids showed remarkable increase in
3-methylhistidine
and beta-amino-isobutyric acid and moderate increase in phenylalanine and arginine. These results revealed that measurement of free amino acid concentration, especially that of methylhistidine as well as myoglobin, pyruvate, lactate and some other enzymes might be of great help to predict the prognosis of patients with acute arterial occlusion of the extremities.
...
PMID:[Metabolic study on acute arterial occlusion of the extremities]. 667 89
