Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.1 (RNase)
 16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Oral administration of one dose of 6.0 and 12.0 mg retinol for one day significantly increased percentage free activities of protease (cathepsins), cathepsin B1 and acid ribonuclease, whereas feeding of one dose of 1.5 mg retinol for one day did not release the above enzymes in younger rats. However, feeding of 1.5, 6.0 and 12.0 mg retinol daily for two days did not significantly increased the percentage free activities of these lysosomal enzymes except that of acid ribonuclease which was still increased in young rats fed 12.0 mg retinol. Retinol feeding either for one day or two days did not affect the release of acid phosphatase and aryl sulphatase in young rats. Retinol inhibited in vitro the activities of protease (cathepsins) and cathepsin B1.
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PMID:Hepatic lysosomal enzymes in young rats fed retinol. 44 49

A cDNA encoding bovine procathepsin B was isolated. The deduced amino acid sequence revealed that a stop (TAG) codon, instead of a Trp-257 codon (TGG), generates in bovine a cathepsin B precursor four amino acids shorter than in other species. Because micro-heterogeneities were previously reported in the cathepsin B primary structure, sequence polymorphism in the protein coding region was then investigated by PCR sequencing of genomic fragments and RNase protection assays. Experiments performed with 12-15 animals of three breeds did not reveal any difference with our cDNA sequence. We conclude that sequence polymorphism in bovine cathepsin B is a rare event, and can only result from the expression of different alleles of a unique gene.
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PMID:Nucleotide sequence of bovine preprocathepsin B. A study of polymorphism in the protein coding region. 837 11