Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous work from this laboratory had indicated that in vivo, histidine decarboxylase (HDC) activity was stimulated by compound 48/80 in rat leg muscle, and that high dietary calcium had a stimulating effect on gastric HDC activity. In the present investigations the 48/80 effect was also observed in vitro in leg muscle extracts from rats, chicks, and guinea pigs. Compound 48/80 had no effect in vitro on histamine metabolism of gastric tissue homogenates in any of the animal species studied. A dietary effect of high calcium intake was noted in rat gastric tissue but not in rat leg muscle. In vitro addition of 48/80 and/or calcium had no stimulatory effect on bacterial HDC or on muscle carnosinase activity. These findings, in conjunction with a comparison of stomach and leg muscle mast cell populations, confirm an HDC stimulatory role for 48/80 in muscle, in addition to its histamine-releasing function from mast cells.
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PMID:Differential response of muscle and gastric histidine decarboxylase to compound 48/80 and dietary calcium. 241 63

A summary is given of experiments performed to study the effects of Maillard reaction products on protein digestion and uptake. A double-isotope technique was used to evaluate the impact of compounds formed in the Maillard reaction on the intestinal uptake of dietary proteins in rats. It was found that low-molecular weight compounds from a glucose-lysine reaction mixture reduced the plasma level of dietary protein-derived lysine. The reaction mixture inhibited in vitro carboxy-peptidase A (E.C. 3.4.17.1) and the brush border enzyme aminopeptidase N (E.C. 3.4.11.2). A glucose-lysine reaction compound, 2-formyl-5-(hydroxymethyl)pyrrole-1-norleucine was found to be a strong competitive inhibitor of aminopeptidase N (Ki = 0.2mM) in vitro. When given to rats (3 mg/g diet), it reduced the plasma level of lysine derived from both dietary free and protein-bound lysine. This compound also inhibited carboxypeptidase A, as did a number of substituted furans and pyrroles.
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PMID:Effect of Maillard reaction products on protein digestion. 250 64

The covalent structure of the rat liver 60 S ribosomal subunit protein L37 was determined. Twenty-four tryptic peptides were purified and the sequence of each was established; they accounted for all 111 residues of L37. The sequence of the first 30 residues of L37, obtained previously by automated Edman degradation of the intact protein, provided the alignment of the first 9 tryptic peptides. Three peptides (CN1, CN2, and CN3) were produced by cleavage of protein L37 with cyanogen bromide. The sequence of CN1 (65 residues) was established from the sequence of secondary peptides resulting from cleavage with trypsin and chymotrypsin. The sequence of CN1 in turn served to order tryptic peptides 1 through 14. The sequence of CN2 (15 residues) was determined entirely by a micromanual procedure and allowed the alignment of tryptic peptides 14 through 18. The sequence of the NH2-terminal 28 amino acids of CN3 (31 residues) was determined; in addition the complete sequences of the secondary tryptic and chymotryptic peptides were done. The sequence of CN3 provided the order of tryptic peptides 18 through 24. Thus the sequence of the three cyanogen bromide peptides also accounted for the 111 residues of protein L37. The carboxyl-terminal amino acids were identified after carboxypeptidase A treatment. There is a disulfide bridge between half-cystinyl residues at positions 40 and 69. Rat liver ribosomal protein L37 is homologous with yeast YP55 and with Escherichia coli L34. Moreover, there is a segment of 17 residues in rat L37 that occurs, albeit with modifications, in yeast YP55 and in E. coli S4, L20, and L34.
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PMID:The primary structure of rat liver ribosomal protein L37. Homology with yeast and bacterial ribosomal proteins. 635 Feb 92

An x-ray diffraction study at 2.8 A resolution has yielded the structure of a complex between bovine carboxypeptidase A (peptidyl-L-amino-acid hydrolase, EC 3.4.17.1) and (-)-2-benzyl-3-p-methoxybenzoylpropionic acid. This substrate is an analogue of N-(p-methoxy)-benzoylphenylalanine, in which the amide NH is replaced by CN2. T. Sugimoto and E T. Kaiser (1979) J. Am. Chem. Soc. 101, 39469--3951] have shown that this complex catalyzes stereospecific exchange of that proton of the CH2 group which is in the R configuration. Our structure of this complex suports the model proposed by Sugimoto and Kaiser and is very similar to the productive peptide binding mode suggested by Lipscomb et al. [Lipscomb, W. N., Hartsuck, J. A., Reeke, G. N., Quiocho, F. A., Bethge, P. A., Ludwig, M. L., Steitz, T. A., Muirhead, H. & Coppola. J. C. (1968) Brookhaven Symp. Biol. 21, 24--90]. The proposed roles of glutamic acid 270 in the proton exchange and the interaction of zinc with the carbonyl group of the substrate are consistent with the observed structure.
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PMID:Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogue. 693 21