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

This review describes several types of genetic polymorphism, which have recently been identified in human urine in our laboratory, and have also been found in other human body fluids such as blood, saliva and semen. These include uropepsinogen, ribonuclease, deoxyribonuclease I (DNase I), deoxyribonuclease II (DNase II), 43-kDa glycoprotein, alpha-L-fucosidase, glutamate pyruvate transaminase, alpha-2-HS-glycoprotein, transferrin and vitamin D-binding protein. Several substances can be detected more easily in urine than in plasma. The concentrations of uropepsinogen, DNase I and DNase II in blood plasma are too low for analysis, whereas those in urine are high enough for easy typing. In practice, DNase I-polymorphism is one of the most useful genetic markers for practical purposes, because of its higher content in various body fluids including urine, a well-balanced gene frequency, and its easy and accurate detectability. Furthermore, several genetic markers previously identified in blood and/or other forensic samples can be phenotyped reproducibly and easily from the corresponding urine samples. Thus, urine, in addition to the convenience and non-invasive nature of its collection, is by no means inferior to blood as a sample source for typing in the field of forensic science. Biochemical and serological typing of genetic polymorphisms present in human urine could offer useful information to practising forensic biologists for forensic individualization of urine samples.
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PMID:Genetic polymorphisms detectable in human urine: their application to forensic individualization. 954 53

Bovine ribonuclease B (RNAse B) and asialofetuin (FETUA) were subjected to in-capillary tryptic digest (Pohlentz et al. Proteomics. 2005, 5, 1758-1763) and the obtained glycopeptides were analyzed, respectively, by nanoelectrospray ionization mass spectrometry and collision-induced dissociation (CID) during the ongoing digest. For RNAse, B glycans of the high-mannose type (Man(4) to Man(9)) attached to either a tetra- or a hexapeptide containing the sole N-glycosylation site of the protein were detected. Glycopeptides derived from all three N-glycosylation sites of FETUA were observed, and the corresponding CID spectra proved the respective glycans to be oligosaccharides of the triantennary complex type. Moreover, an O-glycopeptide carrying Gal-GalNAc at T(280) could be unambiguously identified. An in-solution tryptic/chymotryptic digest of human transferrin (TRFE) was analyzed directly for glycopeptides subsequent to the addition of methanol and formic acid. Disialylated diantennary glycans were observed in glycopeptides of both N-glycosylation sites of TRFE. These results demonstrate the feasibility of direct structure determination of glycopeptides in proteolytic mixtures without any further refurbishment.
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PMID:Structure elucidation of glycoproteins by direct nanoESI MS and MS/MS analysis of proteolytic glycopeptides. 1796 May 75