Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.9 (ribonuclease)
 6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum contains a sugar transferase which is able to catalyse the glycosylation in vitro of the asparagine residue present in the sequence Asn.Leu.Thr in bovine pancreatic ribonuclease. UDP-2-Acetamido-2-deoxy-D-glucose (UDP-N-acetyl-D-glucosamine) acts as a donor, although the mechanism of the transfer is unexplored. Spermidine and Mn2+, as well as CDP-choline, can act as activators for the reaction. Monoglycosylated ribonuclease (ribonuclease-GlcNAc) has been separated (23% yield) from unreacted ribonuclease A by affinity chromatography on a column of wheat-germ agglutinin bound to Sepharose, and characterised. A possible reason for the presence of the enzyme in serum is suggested.
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PMID:UDP-N-acetyl-D-glucosamine-asparagine sequon N-acetyl-beta-D-glucosaminyl-transferase-activity in human serum. 98 74

Oncofetal markers for colon carcinomas are CSAp, a nonsulfated mucin, a second trimester fetal antigen, an altered thymidine kinase, a monosialoganglioside, and glycolipid antigens. For gastric carcinoma, they are basic fetoprotein, a sulfoglycoprotein, and for pancreatic carcinomas--POA, an oncofetal pancreatic antigen, and designated as CAPI, an oncofetal antigen. Tumor-associated markers for colon carcinomas are: UDP-galactosyltransferase and zinc glycinate marker; for gastric carcinomas, sulfated glycoprotein and for pancreatic carcinomas, pancreas carcinoma-associated antigen, a polycytidylic acid-specific ribonuclease, and galactosyltransferase. Suggested as tumor-specific markers for colon carcinomas are an altered mucoprotein, basic antigen, beta 2-microglobulin-associated antigen, and a specific adenosine deaminase; for gastric carcinomas, a specific protein, an antigen with 3-oxyanthranilic acid, and an antigen of unknown origin in gastric secretions; for pancreatic carcinomas, an antigen with molecular weight of 380,000 daltons and an antigen suggested by tumor immunity.
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PMID:Gastrointestinal tumor markers, other than carcinoembryonic antigen, and alpha fetal protein. 688 74

We describe a method for obtaining radioactive fingerprints from nonradioactive ribonucleic acid. Fragments derived by T1 ribonuclease digestion of RNA are dephosphorylated with bacterial alkaline phosphatase. When these fragments are used as primers for the reaction of primer dependent polynucleotide phosphorylase with [alpha-(32)P]GDP in the presence of T1 ribonuclease the 3'-hydroxyl group of each fragment becomes phosphorylated. The degree of phosphorylation is reasonably uniform. The method has been applied to T1 ribonuclease digests of Escherichia coli tRNA(Met) (f); the oligonucleotides were further analyzed by spleen phosphodiesterase digestion. In a similar manner fingerprints of pancreatic ribonuclease digests of RNA can be obtained, when [alpha-(32)P]UDP, polynucleotide phosphorylase and pancreatic ribonuclease are used.
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PMID:Fingerprinting nonradioactive ribonucleic acid with the aid of polynucleotide phosphorylase. 1079 69

1. ADP, ATP and GDP inhibited the phosphotransferase activity, the release of cyclic nucleotides from RNA, of ribonuclease. No significant inhibition was elicited by pyrimidine 5'-nucleoside diphosphates, CDP and UDP. 2. Inhibition by ADP, AMP, adenosine, adenine, NAD and NADP was insignificant at the concentrations tested. Small inhibition was observed with high concentrations of AMP and only when soluble RNA was the substrate. 3. Inhibition by ADP was found to be ;uncompetitive'. 4. Results seem to indicate that at least for optimum inhibition the polyphosphate of the purine nucleoside is essential. They further suggest that the inhibitor acts by combining with the enzyme only when the enzyme is bound to the substrate.
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PMID:Effect of nucleoside 5'-di- and 5'-tri-phosphates on pancreatic ribonuclease activity. 1674 35