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

Several features of carboxypeptidase A (CPA) which were previously established by the X-ray diffraction structure studies have now been confirmed by the chemical sequence analysis. These results include the number (307) of amino acid residues in CPA(alpha), the identities of the residues (Arg 145, Glu 270, and Tyr 248) shown by the X-ray study to be involved in substrate binding and catalysis, and the existence of a disulfide bond. The Zn ligands, shown by the X-ray study to be residues 69, 72, and 196 and identified as His, Glx, and either Glx or Lys, are proved by the chemical sequence to be His, Glu, and His, respectively. No change is required in our previous mechanistic deductions, which are here extended to include a specific mechanism of activation of the substrate by a net charge on the metal ion, which suffers a change in local dielectric constant when it is covered by a substrate.
 ...
PMID:The structure of carboxypeptidase A. IX. The x-ray diffraction results in the light of the chemical sequence. 526 13

A set of chemical reactions was used to show that one glutamic acid residue at the active site of bovine lung angiotensin I-converting enzyme is esterified with the alkylating agent p-[N,N-bis(chloroethyl)amino] phenylbutyryl-L-Pro (chlorambucyl-L-Pro), an affinity label for this enzyme (Harris, R. B., and Wilson, I. B. (1982) J. Biol. Chem. 257, 811-815). The same procedure was used to confirm that a glutamic acid residue of carboxypeptidase A alpha is esterified by reaction with bromoacetyl-N-methyl-L-phenylalanine (Haas, G. M., and Neurath, H. (1971) Biochemistry 10, 3535-3546). In the procedure described in this paper, the esterified residue at the active site is converted to the hydroxamic acid by reaction with hydroxylamine and the hydroxamic acid is subject to the Lossen rearrangement. If a glutamic acid residue was esterified, 1 eq of 2,4-diaminobutyric acid will be formed. Aspartyl esters will give 2,3-diaminopropionic acid. The diamino acids can be quantitatively measured using the short column of an amino acid analyzer if the amount of lysine and histidine is largely decreased by modification with suitable side chain protecting groups. With carboxypeptidase A, the reactions were done on the whole undigested enzyme. With the converting enzyme, we first cleaved the esterified enzyme with cyanogen bromide. Twenty-nine cleavage peptides were separated on high performance liquid chromatography and one of these contained all of the bound radioactive inhibitor. This active site peptide was then subjected to the derivatization and Lossen procedures, and 1 eq of 2,4-diaminobutyric acid was obtained.
 ...
PMID:Glutamic acid is an active site residue of angiotensin I-converting enzyme. Use of the Lossen rearrangement for identification of dicarboxylic acid residues. 613 87

At aseptic inflammation developing around a solid foreign body and proceeding both under common conditions and on the background of disturbed inactivation of free amines as a result of monoaminoxidase blockade with vetrasin or devastation of amine tissue depots with reserpine it has been stated that indices of the adrenal cortex activity (hyperemia, contents of ascorbic acid and corticoids) and those of the mast cells system in the inflammatory focus (amount of the cells, their size, contents of glycosaminoglycans, RNA, tryptophan and histidine) are subjected to certain fluctuations during inflammation. Increasing activity of the adrenal cortex fascicular zone and renewal of the mast cell population in the inflammatory focus are directly proportional to the degree of a disturbed deposition of free amines in the organism. Certain positive correlations prevail in cooperation of the adrenal cortex activity, decomposition rate of large (mature) mast cells and migration into the inflammatory focus of small (immature) forms of these cells.
 ...
PMID:[Connections between the mast cell system of a focus of inflammation and the zona fasciculata of the adrenal cortex]. 617 98

In vitro exposure of mast but not of other cells of rat peritoneal fluid to epinephrine leads, within 1 min, to progressing levels of histamine in both fluid and sedimentable phases of the incubates, which present no increase in their free/total histamine ratio. Histamine increase was blocked by alpha-fluoromethyl histidine (alpha FMH), acting after a significant lag period. When compared with controls under the electron microscope, epinephrine-treated mast cells show less electron-dense, swollen intracellular granules, apparent maintenance of cell membrane continuity and an apparent decrease of peripheral finger-like projections. Histamine accumulation by epinephrine-treated mast cells may be the result of an enhanced ability of pre-formed mast cell histidine decarboxylase to attack its cell-borne substrate, consequent to an unfolding of the cell membrane during cell tumefaction evoked by epinephrine.
 ...
PMID:Stimulation by epinephrine of histamine synthesis by rat peritoneal fluid mast cells in vitro. 620 9

Four low-molecular-mass polypeptides were isolated and purified from chromatophore membranes of Rhodopseudomonas sphaeroides blue-green mutant R-26.1 by a combination of gel filtration and ion-exchange chromatography in organic solvents. On dodecyl sulfate polyacrylamide gels, the purified polypeptides comigrate with bands LH-1, LH-2 and LH-3 known to be related to the antenna-pigment-protein complexes. The complete primary structures were elucidated by automated Edman degradation of the intact polypeptides and of overlapping C-terminal fragments obtained after chemical cleavage at tryptophan and methionine residues. The C-termini were verified by hydrazinolysis and, in one case where an overlapping C-terminal fragment could not be obtained, by digestion with carboxypeptidase A. The four polypeptides show a tripartite structure: i.e. a polar N-terminal region is separated from a polar C-terminal region by a segment of about 21 predominantly hydrophobic amino-acid residues. All hydrophobic segments contain a characteristic conservative histidine residue. The C-terminal region is reduced to only a few amino acids in the two polypeptides which together form band LH-3, i.e. LH-3A and LH-3B. Their extended N-terminal region is rich in charged residues and contains an additional conserved histidine residue close to the beginning of the hydrophobic segment. These properties place LH-3A and LH-3B into subgroup (beta-polypeptides: B 870-beta and B 850-beta, respectively). LH-1 and LH-2 appear to form another subgroup (alpha-polypeptides: B 870-alpha and B 850-alpha, respectively) as suggested during a search for conservative elements within their sequences (structural basis for classification). N-Terminal analyses carried out with intact antenna-pigment-protein complexes revealed the following: (i) LH-1 and LH-3 are associated with the B 870 complex in Rp. sphaeroides 24.1 (wild type), (ii) the same polypeptides are almost exclusively present in chromatophore membranes of Rp. sphaeroides R-26, a blue-green mutant which absorbs at 870 nm, (iii) LH-2 and LH-3B are the constituent polypeptides of the B 800-850 complex of Rp. sphaeroides 2.4.1 and of the spectrally altered B 850 complex isolated from the blue-green mutant R-26.1 which absorbs at 860 nm. This mutant contains LH-2 and LH-3B along with LH-1 and LH-3A and apparently is able to form both types of antenna complexes.(ABSTRACT TRUNCATED AT 400 WORDS)
 ...
PMID:The light-harvesting polypeptides of Rhodopseudomonas sphaeroides R-26.1. I. Isolation, purification and sequence analyses. 638 9

Reexamination of the molecular mass and the amino acid composition of Serratia protease revealed the presence of 1 mol of methionine per mol of protein (about 46K daltons), and this was confirmed by BrCN cleavage followed by separation of the two fragments. The sole methionine residue was located near the middle region of the molecule. The amino(N)-terminal sequence was determined by Edman degradation of the protein and studies of several proteolytic peptides, establishing a sequence of 18 residues with a heterogeneous N-terminus. The carboxyl(C)-terminal sequence was determined by carboxypeptidase A digestion and tritium-labeling of the citraconylated C-terminal half segment to be -Phe-Ile-Val. The sequences of a total of 53 residues containing the methionine residue and a total of 38 residues containing two histidine residues were established by the application of various conventional methods to a BrCN peptide and several proteolytic peptides. The segment containing the histidine residues was homologous with that containing the two histidine residues chelating the zinc atom of thermolysin. The 38-residue segment may be directly connected to the 53-residue segment.
 ...
PMID:Serratia protease. Amino acid sequences of both termini, the 53 residues in the middle region containing the sole methionine residue, and a probable zinc-binding region. 639 98

The uptake and elimination of radiolabelled histamine was studied in the rat duodenum, where histamine is stored in a specific population of mucosal mast cells (MMC), and in the tongue, where histamine is stored in the classic connective tissue mast cell (CTMC). The specific activity of histamine was measured after one i.v. injection of its precursor, 3H-histidine. Decarboxylation of histidine and uptake of histamine occurred in both tissues. The initial specific activity of histamine was very low in the tongue but 5 times higher in the duodenum, while the endogenous duodenal histamine content was 1/6 of that in the tongue. The elimination rate of labelled histamine in the two mast cell pools was very slow. In the tongue, there was no statistically significant decrease in specific activity during the observation period of 16 days. In the duodenum, there was an exponential decrease of prelabelled histamine with an apparent half-life of 9 days. However, part of this decay of radioactivity may be accounted for by increase in the mucosal histamine pool size and MMC death. The results indicate that the rate of histamine elimination from mast cells of both types is very slow, corresponding with previous results obtained from CTMC of the peritoneal cavity.
 ...
PMID:Turnover of different mast cell pools of histamine in the rat. 647 58

A flavin peptide from Corynebacterium sarcosine oxidase was obtained by proteolytic digestion with trypsin and chymotrypsin, and purified by the method of Kenney et al. (1). Amino acid analyses of the flavin peptide gave the following results: Asx(1), Ala(1), Val(1), and His(1) per flavin group. By carboxypeptidase A digestion and partial acid hydrolysis, the structure of the flavin peptide was determined as (Formula: see text).
 ...
PMID:Amino acid sequence around the covalently-bound flavin prosthetic group of Corynebacterium sarcosine oxidase. 667 34

Compositional analysis of the soluble tryptic peptides representing about 70% of the 293 residues of sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster reveals a single peptide difference between the sn-glycerol-3-phosphate dehydrogenase adult (GPDHF-1) and larval (GPDHF-3) isozymes. This peptide was shown to be the carboxyl terminus by sequence determination and by carboxypeptidase A digestion of the native protein. For GPDHF-1, the sequence of the COOH-terminal tryptic peptide is Asn-His-Pro-Glu-His-Met-Gln-Asn-Leu-COOH, while that of GPDHF-3 is Asn-His-Pro-Glu-His-Met-COOH.
 ...
PMID:Structural analysis of adult and larval isozymes of sn-glycerol-3-phosphate dehydrogenase of Drosophila melanogaster. 679 37

Diets containing egg white, casein, menhaden fish meal, soy protein or wheat gluten were fed to rats to assess the impact of dietary protein (and other nutrients) on gastric functions. The menhaden fish meal group exhibited increases in stomach histidine decarboxylase (HDC) activity, histamine concentration, as well as acid secretion when compared with the control, casein group. When rats were fed amino acid-supplemented casein or fish meal diets to simulate each other's amino acid profile, a small increase in gastric HDC activity, histamine content and acid secretion was observed in comparison with the unsupplemented casein or fish meal groups. The high mineral content of menhaden fish meal (15%) was thought to be a potential inducing factor for gastric histamine metabolism and acid secretion. Adding fish meal ash to the casein diet or to a cod fillet diet elevated stomach HDC activity and histamine concentration significantly. Furthermore, when calcium (Ca) was added to the casein diet to simulate its high content in menhaden fish meal (7.8%), similar elevated levels of gastric histamine were obtained for the Ca-supplemented casein group as for the fish meal group. The role of Ca could be due to release of gastrin, which results in release of stomach histamine, or by facilitating mast cell histidine incorporation with subsequent histamine synthesis.
 ...
PMID:Gastric histamine metabolism and acid secretion in rats as influenced by diet and nutrient content. 682 9


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>