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)

A neutral SH-dependent proteinase was isolated from bovine spleen by a slight modification of the previous method (1) and its action on some natural and synthetic substrates was studied. The activity of the enzyme was increased 2000--2500-fold as compared to that of the original extract. The enzyme hydrolyzed various histones (H1, H2a, H2b, H3), casein and protamine but did not split hemoglobin, serum albumin and 14C-tryptophane-labelled total protein from chicken embryos. The enzyme possessed neither collagenolytic nor elastase activity; it did not inactivate aldolase, hexokinase, glyceraldehyde phosphate dehydrogenase and glucose-6-phosphate dehydrogenase, which makes the enzyme different from cathepsin B1 and some other previously described proteinases. The enzyme did not split BAPA, BAEE, ATEE, Boc-Ala-ONP, Leu-beta-NA and some other peptides. The molecular weight of the enzyme was found to be about 15 000.
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PMID:[Isolation and properties of neutral SH-dependent proteinase from bovine spleen]. 43 66

Rat muscle was extracted at pH 4 and submitted to gel-filtration on Sephadex G-75 and to chromatography on DEAE-Sephadex. Gel-filtration gave a large peak of activity towards Bz-Arg-NNap with an estimated molecular weight of 25,500. Activity towards Bz-Arg-NH2 was present in this peak and in another peak of molecular weight 45,000. The second peak also hydrolysed benzoyl-glycyl-L-arginine. DEAE-Sephadex gave five peaks of Bz-Arg-NNap hydrolysing activity; all showed thiol dependence. Peaks III, IV and V hydrolysed Z-Ala-Arg-Arg-NNap-OMe rapidly; they also inactivated aldolase and were strongly inhibited by leupeptin. They are probably isoenzymes of cathepsin B1. Peak I showed these properties to a relatively small extent. 7-(N-Benzoyl-DL-argininamide)-4-methylcoumarin appears to be an alternative substrate for cathepsin B1; it was hydrolysed also by peak I, but relatively less rapidly. Peaks I and II were inhibited more than peaks III, IV and V by a muscle extract. Total activity of the Bz-Arg-NH2-hydrolysing enzyme in extensor digitorum longus muscle increased after denervation.
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PMID:Separation of cathepsin B1 and related enzymes from rat skeletal muscle. 45 46

The activities of serine protease, cathepsin B1, ornithine aminotransferase, and aldolase in skeletal muscles of mice with hereditary muscular dystrophy and their normal litter mates were studied. In dystrophic muscle, the specific and total activities of serine protease were much higher than in normal muscle, and the specific activities, but not the total activities, of cathepsin B1 and ornithine aminotransferase were twice those in normal muscle, and several new fragments, which are normally formed by limited proteolysis, were found in dystrophic muscle. When myofibrillar proteins of normal and dystrophic muscles were incubated with highly purified serine protease, their myosin, alpha-actinin and tropomyosin disappeared completely.
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PMID:Serine protease in mice with hereditary muscular dystrophy. 62 6