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)

Using fluoresceine isothiocyanate labeled protamine sulfate it is possible to stain rat mast cell fractions of isolated periotoneal cells in a selective way. The cells are not degranulated, though they have lost their histamine completely. The method shows the dissociation of the mediator release and the extrusion of the granules.
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PMID:Fluorescence microscopical visualization of rat mast cells by means of fluoresceine isothiocyanate labeled protamine sulfate. 8 58

Angiotensin-converting enzyme has been solubilized from a particulate fraction of rabbit lung and purified to apparent homogeneity in 11% yield by a procedure including fractionation with DEAE-cellulose and calcium phosphate gel, elution from Sephadex G-200, and lectin affinity chromatography. The molecular weight estimated by equilibrium sedimentation was approximately 129,000, either in the absence or presence of 6 M guanidine hydrochloride. A slightly higher value of 140,000 determined for the reduced, denatured protein by gel electrophoresis in the presence of sodium dodecyl sulfate and a much higher figure derived from gel filtration are probably due to the glycoprotein nature of the enzyme. Its oligosaccharide content accounted for 26% of the weight calculated from its amino acid and carbohydrate composition. The estimated content of sugar residues per mole was: galactose, 57; N-acetylglucosamine, 53; mannose, 43; N-acetylneuraminic acid, 19; and fucose, 4. Threonine and alanine were identified, respectively, as NH2-terminal and COOH-terminal residues by the dansylation procedure and by digestion with carboxypeptidase A. The enzyme was found to contain approximately 1 g atom of zinc per mol. Km values for hydrolysis of hippurylhistidylleucine and angiotensin I were 2.3 and 0.07 mM, and the corresponding turnover numbers were 15,430 and 792 mol/min/mol at 37 degrees. Bradykinin was also a substrate, and release of its COOH-terminal dipeptide, Phe-Arg, was catalyzed at a comparable rate to that of His-Leu from the COOH terminus of angiotensin I. Enzyme activity required the presence of chloride ions and was inhibited by EDTA and by low concentrations of Bothrops bradykinin-potentiating peptides. In addition, hydrolysis of hippurylhistidylleucine was inhibited competitively by other defined peptides, including di- and tripeptides, which were not substrates.
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PMID:Pulmonary angiotensin-converting enzyme. Structural and catalytic properties. 16 57

High density lipoproteins were isolated from plasma of white Leghorn hens by ultracentrifugal flotation between densities 1.063 and 1.210 g/ml. After delipidation, the lipid-free proteins were fractionated by chromatography on Sephadex G-150 in urea; one major apolipoprotein was isolated and characterized. From its chemical, physical and immunochemical properties, the major apoprotein from hen high-density lipoproteins has characteristics similar to the major apoprotein of human high density lipoproteins, apoA-I. Thus the hen protein has been designated hen apoA-I. Hen apoA-I has a molecular weight of approximately 28 000 as determined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Its calculated molecular weight from its 234 constituent amino acids is 26 674. Hen apoA-I differed from its human counterpart by containing isoleucine. Treatment of hen apoA-I with carboxypeptidase A yielded a COOH-terminal sequence of Leu-Val-Ala-Gln. Automatic Edman degradation of the apoprotein gave an NH2-terminal sequence of Asp-Glu-Pro-Gln-Pro-Glu-Leu. Hen apoA-I had a circular dichroic spectrum typical of alpha-helical structures; the calculated helicity was 90%. Goat antisera prepared to hen apoA-I formed precipitin lines of complete identity to the hen apoprotein but lines of only partial identity to human apoA-I. These studies show that the major apoprotein from hen and human high-density lipoproteins have similar properties to each other suggesting a common physiologic function.
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PMID:Isolation and characterization of the major apolipoprotein from chicken high density lipoproteins. 17 37

Baboon high-density lipoproteins (HDL) were isolated by preparative ultracentrifugation between d = 1.063 and 1.215 g/mL. The HDL contains 48.8% protein and a lipid distribution similar to human HDL. The phospholipid distribution shows a low sphingomyelin value (5.9%), and the fatty acid composition of HDL is comparable to the human data except for the 18:1/18:2 ratio as a result of a higher 18:1 content in the CE and a lower 18:2 concentration in the PL. The major HDL apoproteins isolated on diethylaminoethyl-cellulose had a mobility on sodium dodecyl sulfate--polyacrylamide gel electrophoresis and a molecular weight and an amino acid composition similar to human apoA-I. However, the amino acid sequence of the first 30 residues of baboon apoA-I differed from the human apoprotein in residues 15 and 21. Treatment of apoA-I with carboxypeptidase A indicated a carboxyl-terminal sequence of Leu-Ser-Thr-Gln. Baboon apoHDL contained monomeric apoA-II with the mobility of monomeric human apoA-II and a molecular weight of 8500. The amino acid composition differed from the human apoA-II by the presence of arginine and by the absence of half-cystine and isoleucine. The circular dichroic spectra of apoA-I and apoA-II demonstrated a higher helicity compared to the human apoproteins. Recombination studies by microcalorimetry of apoHDL with dimyristoylphosphatidylcholine (DMPC) indicated similarities in the thermodynamic binding properties of the HDL apoproteins from man and baboon. The maximal-binding enthalpies of DMPC to apoHDL, apoA-I, and apoA-II were lower for the baboon than for the human apoprotein.
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PMID:Characterization of baboon plasma high-density lipoproteins and of their major apoproteins. 19 55

Polypeptide VII of cytochrome c oxidase was isolated and purified by gel filtration on Bio-Gel P-10 in 10% acetic acid. Automatic Edman degradation of this peptide chain was not successful, because it is blocked at the N-terminus. The amino acid analysis shows a relatively high content of hydrophilic residues (54%). On the basis of this analysis and the apparent molecular weight by sodium dodecyl sulfate gel electrophoresis and gel filtration, a chain length of about 80 residues was calculated. Among the tryptic peptides one blocked heptapeptide was found. Cleavage of this peptide with thermolysin gave two peptide fragments, one of which was not retained on a cation exchange resin. Mass spectrometric sequence determination of this peptide revealed the structure Ac-Ala-Glu-Asp for the N-terminus of polypeptide VII. Treatment with carboxypeptidase A at two different pH values showed that the C-terminal amino acid is isoleucine and the penultimate amino acid is lysine.
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PMID:Studies on cytochrome c oxidase, VII. Isolation and chemical characterization of polypeptide VII. 22 66

1. All the porcine pancreas enzymes tested, regardless of their pI's were adsorbed on Amberlite CG-50 (a weakly acidic cation exchange resin) at pH 4, where the ion-exchange group (carboxyl group) is not dissociated. The adsorption is hardly influenced by ionic strength. 2. At pH 4, the adsorbed enzymes were partially eluted by organic solvents such as 50% propanol. 3. The adsorbed enzymes were effectively eluted by increasing the pH from 4 to 6. Trypsin (pI 10.5) was eluted before carboxypeptidase A (pI 4.5 AND 5.3) WITH 0.5 M acetate buffer, whereas the former enzyme was eluted after the latter enzyme with 0.2 M 3,3-dimethyl glutarate buffer. However, with either buffer, the elution order of enzymes was not always the same as the order of the pI's. 4. By a single Amberlite CG-50 column chromatography of porcine pancreas extracts, kallikrein, carboxypeptidase B, deoxyribonuclease, carboxypeptidase A, and trypsin were purified 100-fold, 16-fmately 13%. The purification procedures included treatment with protamine, ammonium sulfate fractionation, treatment with acid, DE-32 cellulose column chromatography, gel filtration on Sephadex G-100, preparative polyacrylamide gel electrophoresis, and affinity chromatography on 5' AMP-Sepharose 4B. The last procedure, affinity chromatography on 5' AMP-Sepharose 4B, was useful for the removal of other dehydrogenases. The enzyme which was homogeneous, as shown by polyacrylamide gel electrophoresis, had a molecular weight of about 92,000. The optimum pH was at 10.0 and isoelectric point at 5.2. The enzyme accepted both L-fucose and D-arabinose as substrate, but was specific for NAD+ as coenzyme. Km values were 0.15 mM, 1.4 mM, and 0.07 mM for L-fucose, D-arabinose, and NAD+, respectively. A single enzyme catalyzed the oxidation of L-fucose and D-arabinose, which had the same configurations of hydroxyl groups from C-2 to C-4. The reaction products obtained with L-fucose as substrate were L-fucono-lactone and L-fuconic acid. The L-fucono-lactone was an immediate product of oxidation and was hydrolyzed to L-fuconic acid spontaneously. This reaction was irreversible. Therefore, it is likely that L-fucose dehydrogenase is involved in the initial step of the catabolic pathway of L-fucose in rabbit liver.
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PMID:Hydrophobic-ionic chromatography. Its application to purification of porcine pancreas enzymes. 31 32

In an attempt to ascertain whether opiate receptors and brain enkephalins or endorphins are involved in pentobarbital anesthesia and toxicity, the effects of 1) two pure narcotic antagonists, naloxone and naltrexone, 2) morphine sulfate, 3) D-phenylalanine, an inhibitor of carboxypeptidase A, and 4) D-leucine, an inhibitor of leucineaminopeptidase, in combination with D-phenylalanine, were studied in mice. Both naloxone and naltrexone, (1, 5 and 10 mg/kg) administered subcutaneously to mice were unable to modify the duration of anesthesia when they were injected 5 min prior to a challenge dose (75 mg/kg) of pentobarbital (ip). The onset of anesthesia was unaltered by naloxone (1, 5 and 10 mg/kg) and naltrexone (1 mg/kg). Higher doses of naltrexone (5 and 10 mg/kg) delayed the onset of anesthesia slightly. Morphine (1, 2.5 and 5 mg/kg) given 30 min before pentobarbital did not modify the onset or the duration of anesthesia. D-Phenylalanine (250 mg/kg), and D-phenylalanine + D-leucine (250 mg/kg each) injected ip an hour before pentobarbital did not affect either onset or duration of anesthesia. Naltrexone (10 mg/kg, ip) given 5 min before pentobarbital did not alter the LD50 of the latter. The studies do not support a role of enkephalins or endorphins in pentobarbital anesthesia or toxicity, and suggest a need for caution in using narcotic antagonists in treating pentobarbital toxicity.
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PMID:Studies of the possible role of brain endorphins in pentobarbital anesthesia and toxicity in mice. 49 53

Microtubules from the cow adrenal cortex and brain were purified by three cycles of the temperature-dependent polymerization-depolymerization procedure. Whereas tubulin comprised approximately 8--10% of soluble brain protein, it comprised only 0.5-1.0% of the soluble adrenocortical protein. The partially purified tubulin from both sources gave similar results in the following studies: (1) [3H]colchicine binding examined by Scatchard analysis revealed an apparent Ka of 1 . 10(6) M-1 and a colchicine/tubulin molar binding ratio of 0.4-0.6; (2) tyrosylation studies using a specific tubulin-tyrosine ligase (which adds a tyrosine residue to the C-terminal glutamate or glutamine of the alpha-chain) in conjunction with carboxypeptidase A (which recovers the tyrosine) and (3) amino acid analysis. Examination of protein bands, in addition to the tubulin doublet of 55 000 molecular weight, on sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed a difference between the two tubulin preparations. The adrenocortical preparation had protein bands corresponding to apparent molecular weight of 36 000, 60 000, and 68 000. In contrast the brain preparation had only proteins of molecular weights greater than 200 000 (these bands were absent in all adrenal preparations). It would thus appear that if proteins which copurify with tubulin through repeated cycles of polymerization-depolymerization play a role in either microtubule formation or function there is a distinct difference between neural and non-neural tissue.
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PMID:Purification of bovine adrenocortical and brain tubulin. A comparative study. 50 97

The early membrane events taking place during mast cell secretion were followed in transmission and freeze-fracture electron microscopy. In order to slow down exocytosis and capture intermediate stages of membrane fusion, special conditions of incubation and stimulation were used. These were as follows: (a) the use of incubation media with altered ionic composition, and (b) stimulation with a low dosage of polymyxin B sulfate (4 microgram/ml) at low temperature (18 degrees C) for very short incubation times (30-60 s), with or without the presence of formaldehyde (0.8%). Under these conditions, unetchable circular impressions are found on the E face of the plasma membrane, 80-100 nm in diameter, with particles associated with their perimeters. In granule-to-granule fusion, the zone involved is demarcated by one or two rows of particles on the E face. In addition, raised circular areas of varying diameters (43-87 nm) surrounded by similar particles, also found on the E face, may represent potential sites before completion of fusion. Neither the circular impressions on the plasma membrane nor the sites on the granule membrane are permanent, but their appearance coincides with initiation of membrane fusion.
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PMID:A freeze-fracture study of early membrane events during mast cell secretion. 55 77

Anaphylactoid reactions to protamine sulfate have been attributed to its capacity for nonimmunologic mast cell degranulation and/or complement consumption. In the current study, evidence is presented for the occurrence of an immunologic anaphylactic reaction mediated by a complement-dependent IgG skin-sensitizing antibody. A retrospective study of blood component donors given protamine for heparin neutralization revealed that prior exposure to protamine is associated with increased risk of adverse reaction to the drug.
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PMID:Anaphylaxis to protamine sulfate mediated by a complement-dependent IgG antibody. 62 46


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