Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A complete amino acid sequence has been determined for the UP1 single-stranded DNA binding protein from calf thymus that was first described by G. Herrick and B. M. Alberts [(1976) J. Biol. Chem. 251, 2124-2132]. Peptides required to establish the UP1 sequence were isolated by reversed-phase HPLC of digests produced by endoproteinase Lys-C, trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide cleavage of UP1. The purified peptides were coupled to aminopolystyrene prior to solid-phase sequencing. UP1 contains 195 amino acids and has a molecular weight of 22,162. UP1 has a blocked NH2 terminus and contains a single NG,NG-dimethylarginine residue near its COOH terminus. Gas-phase sequencing of tryptic peptides derived from an analogous protein from mouse myeloma cells [Planck, S. R. & Wilson, S. H. (1980) J. Biol. Chem. 255, 11547-11556] revealed that this mouse helix-destabilizing protein shares a high degree of sequence homology with UP1. Of the 59 amino acids in the mouse protein that have so far been found to be homologous with UP1, 48 correspond exactly to sequences found in UP1. Most of the 11 differences that have been found between the sequences of these two proteins are conservative in nature, involving primarily the interchange of chemically similar amino acids. One 9-residue mouse sequence that is not obviously homologous to UP1 may be a result of the larger size of the mouse myeloma protein as compared to UP1. Since none of the UP1 or mouse myeloma helix-destabilizing protein sequence appears to be homologous to that of any previously sequenced protein, we presume that these two proteins represent a distinct class of single-stranded nucleic acid binding proteins that probably play a role in metabolism of single-stranded RNA or DNA in vivo.
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PMID:Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma. 299 41

In order to elucidate the biological role of NG,NG-dimethylarginine dimethylaminohydrolase (EC 3.5.3.18), we prepared monoclonal antibodies (mAbs) against the enzyme from rat kidney and examined the distribution of the enzyme in rats. Four mAbs have been obtained by the fusion of the spleen cells from BALB/c mouse immunized with the sodium dodecyl sulfate-denatured or native enzyme and P3X63Ag8U1 myeloma cells. All the mAbs were shown to bind to the denatured enzyme, but none of them could recognize the native enzyme. The occurrence of the enzyme protein in various rat tissues and cell systems such as peritoneal neutrophils and macrophages was examined using an immunoblotting technique with one of the mAbs. The immunoblotting analyses showed that the enzyme protein is widely distributed in rats, particularly, in kidney, pancreas, liver, brain, and aorta at high concentrations. Furthermore, the enzyme protein was clearly shown to exist in peritoneal neutrophils and macrophages. Since NG-monomethylarginine and NG,NG-dimethylarginine have been suggested to be specific blockers of the systems generating nitric oxide (NO), the above findings are of great interest in connection with the regulation of the NO production in such tissues and cell systems as aorta, brain, peritoneal neutrophils, and macrophages.
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PMID:Detection of NG,NG-dimethylarginine dimethylaminohydrolase in the nitric oxide-generating systems of rats using monoclonal antibody. 843 46