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)

A technique utilizing Pregnant Mare's Serum Gonadotropin and Human Chorionic Gonadotropin treatment of hens (Gallus domesticus), followed by manual ovulation of the excised follicles, was developed to obtain a large number of mature ova. The intact ova were used to test whether acrosin, partially purified from the spermatozoa of the cock (Gallus domesticus), partially purified rabbit testicular acrosin and commercial preparations of several hydrolytic enzymes could dissolve the inner vitelline membrane. Enzymes were applied to pieces of filter paper placed on the ovum. Cock acrosin and endopeptidases such as trypsin, chymotrypsin, collagenase and elastase hydrolyzed the membrane whereas exopeptidases such as leucine aminopeptidase and carboxypeptidase A did not. Phospholipase A, sulfatase, hyaluronidase, beta-glucuronidase and rabbit testicular acrosin also failed to hydrolyze the membrane. Cock acrosin hydrolysis of the ovum surface was inhibited by soybean trypsin inhibitor. The surface of the ovum over the germinal disc region was hydrolyzed more quickly by cock acrosin than the surface over other regions of the ovum. Acrosin from cock sperm caused the release of trichloroacetic acid soluble material absorbing at 280 nm from sonicated preparations of inner vitelline membranes. Hydrolysis was greatest at pH 8.0 and was inhibited by soybean trypsin inhibitor.
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PMID:Hydrolysis of the hen egg vitelline membrane by cock sperm acrosin and other enzymes. 0 Apr 54

Large quantities of the low-molecular-weight natriuretic material (F4), which appears after the salts when fractionated on G-25 Sephadex column, were obtained from the urine of normal man on a normal diet. The natriuretic substance in F4 was (1) untrafiltrable through a membrane with a claimed molecular-weight cut-off of 500 daltons (Amicon UMO5); (2) soluble in more polar organic solvents; (3) totally soluble in 95% acetone when specific activity was doubled; (4) relatively resistant to heating at 100 degrees C for 1 hour at a pH of 10, and to heating at 110 degrees C in 6 N hydrochloric acid for up to 90 hours under anaerobic conditions, and treatment with nitrous acid; it was less resistant to these procedures when extracted into 95% acetone; (5) not destroyed by trypsin, chymotrypsin, pronase, pepsin, leucine aminopeptidase, and subtilysin, nor was it destroyed by pepsin, leucine aminopeptidase, subtilysin, carboxypeptidase A and B, and aminopeptidase M, or by monoamine oxidase, aryl sulphatase, and beta-glucuronidase when extracted into 95% acetone. The natriuretic substance in the 95% acetone-soluble F4 was totally destroyed by incubation with prolidase. The least amount of 95% acetone-soluble F4 required to produce a significant natriuresis in the bioassay rat was that derived from a 7-min sample of urine. The maximal response was obtained from a 30-min sample of urine. Continuous i.v. infusion of the 95% acetone-soluble F4 for 40 min produced a sustained natriuresis, whereas a greater amount injected as a bolus produced an effect which was not sustained beyond 20 min.
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PMID:Further observations on a low-molecular-weight natriuretic substance in the urine of normal man. 4 87

From mouse spinal cord homogenate, we isolated a trophic substance which reverses the post-denervation decrease in tetrodotoxin sensitivity of action potential in organ-cultured extensor digitorum longus muscle of mouse and characterized its physicochemical properties. The trophic substance was separated from macromolecules in homogenate by gel filtration on Biogel P2 column. The partially purified trophic substance was heat-stable, acid-stable and alkaline-labile. The trophic activity was destroyed by lyophilization at neutral pH but not at acidic pH. The trophic activity was abolished by incubation with pronase or leucine aminopeptidase, but not by trypsin, chymotrypsin, thermolysin or carboxypeptidase A. The trophic substance passed through an ultrafiltration membrane UM10 freely. A small part of the trophic activity passed through a UM2 or UM05, and the rest was retained on the membranes. The trophic substance adsorbed on CM-Sephadex at pH 7.2 but passed through DEAE-Sephadex at pH 8.4. These results suggest that the trophic substance regulating tetrodotoxin sensitivity of action potential in mouse skeletal muscle is a peptide with a rather low molecular weight of less than 10,000 and that while the N-terminus of the peptide is free, the C-terminus is probably blocked. This peptide differs from other trophic substances reported previously by other investigators.
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PMID:Partial purification and characterization of neutrophic substance affecting tetrodotoxin sensitivity of organ-cultured mouse muscle. 48 37

Lyophilized bovine, porcine, and human choroid plexuses contain .02-.09 U of antidiuretic activity per milligram. The antidiuretic factor in bovine choroid plexus was concentrated 100 times by extraction with acetic acid, fractional precipitation with acetone and ethyl ether, gel filtration, and paper chromatography. Resulting choroid plexus fraction IIgammaB2 was eluted from Sephadex G-25 in position corresponding to molecular weight between 750 and 3,500; its antidiuretic activity was destroyed by trypsin, performic acid, and thioglycollic acid, but was not affected by leucine aminopeptidase, carboxypeptidase A or B, or cyanogen bromide. HgammaB2 possesses antidiuretic, pressor, and oxytocic potencies (measured in anesthetized-hydrated rat, anesthetized rat, and isolated rat uterus, respectively) of 1.9, 0.5, and 0.1 U/mg, respectively.
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PMID:Antidiuretic peptide in mammalian choroid plexus. 81 22

epsilon-(gamma-Glutamyl)lysine has been found in human stratum corneum in the fraction containing the alpha helical fibrous proteins (keratins) and other high molecular weight proteins. The S-carboxymethylated fractions were enzymatically digested with pronase, carboxypeptidase A and B, leucine aminopeptidase and prolidase, and epsilon-(gamma-glutamyl)lysine isolated from digests by gel filtration and cation ion exchange chromatography. Acid hydrolysis of the purified epsilon-(gamma-glutamyl)lysine yielded equimolar amounts of lysine and glutamic acid, and end group analysis of the peptide by dansylation (application of 5-dimethylaminonaphthalene-1-sulfonyl) confirmed the isomer assignment to be epsilon-(gamma-glutamyl)lysine. About 9 nmol of the peptide per mg of protein were found in the fraction by isotope dilution after the enzymatic digestion. These results suggest that proteins in stratum corneum may be covalently cross-linked through epsilon-(gamma-glutamyl)lysine bonds.
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PMID:epsilon-(gamma-Glutamyl)lysine cross-links in human stratum corneum. 84 47

The enzymic hydrolysis of some proteins (insulin-B-chain-S-sulfonate, S-aminoethylated lysozyme, bovine serum albumin) by immobilized peptidolytic enzymes is reported. Sepharose-bound pronase, trypsin and a protease from Thermoactinomyces sp. (MP), the latter both cross linked by glutaric dialdehyde and an exopeptidase mixture containing Sepharose-bound leucine aminopeptidase, carboxypeptidase A and a crude preparation of prolidase were used. After enzymic hydrolysis nearly all amino acids, except proline, were recovered in a 100% yield compared to the value of an acid reference hydrolysate. Tryptophan and methionine, which are partially destroyed by acid hydrolysis in the presence of oxygen could be recovered completely.
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PMID:[Protein hydrolysis by immobilized enzymes]. 98 21

The fluorescence emission and chemical reactivity of soluble and Sepharose-bound leucine aminopeptidase and carboxypeptidase A were investigated and the results compared. Both natural fluorescence and the fluorescence of fluorescein-labeled enzymes were utilized. The front-surface viewing technique enables us to measure the apparent fluorescence quantum yields and the rotational relaxation times of fluorescent groups within native unbound and carrier-fixed enzymes. The chemical reactivity was probed with Ellman's reagent and iodoacetic acid. Both types of methods were found to be useful in detection and quantitation of matrix-induced alterations in immobilized enzymes.
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PMID:Fluorescence and chemical reactivity as empirical indices of matrix-induced alterations in immobilized enzymes. 118 29

A phosphonamide peptide, N-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid, previously shown to block Clostridium histolyticum collagenases, was examined as a putative inhibitor of endopeptidase 24.16 and endopeptidase 24.15. Hydrolysis of two endopeptidase 24.16 substrates, i.e. 3-carboxy-7-methoxycoumarin (Mcc)-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl (Dnp) and neurotensin, were completely and dose-dependently inhibited by the phosphonamide inhibitor with KI values of 0.3 and 0.9 nM respectively. In addition, the phosphonamide peptide inhibited the hydrolysis of benzoyl (Bz)-Gly-Ala-Ala-Phe-(pAB) p-aminobenzoate and neurotensin by endopeptidase 24.15 with about a 10-fold lower potency (KI values of 5 and 7.5 nM respectively). The selectivity of this inhibitor towards several exo- and endo-peptidases belonging to the zinc-containing metallopeptidase family established that a 1 microM concentration of this inhibitor was unable to affect leucine aminopeptidase, carboxypeptidase A, angiotensin-converting enzyme and endopeptidase 24.11. The present paper therefore reports on the first hydrophilic highly potent endopeptidase 24.16 inhibitor and describes the most potent inhibitory agent directed towards endopeptidase 24.15 developed to date. These tools should allow one to assess the contribution of endopeptidase 24.16 and endopeptidase 24.15 to the physiological inactivation of neurotensin as well as other neuropeptides.
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PMID:Potent inhibition of endopeptidase 24.16 and endopeptidase 24.15 by the phosphonamide peptide N-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid. 133 78

Melanin-concentrating hormone (MCH) is a cyclic peptide which behaves as an antagonist of the pituitary melanotropic hormone alpha-melanocyte-stimulating hormone in fishes. Cloning of the rat MCH cDNA precursor recently revealed the presence of an additional putative peptide named NEI. The present work examined the susceptibility of these novel peptides to hydrolysis by various purified exo- and endo-peptidases including endopeptidases 24.11 (NEP), 24.15, 24.16, angiotensin-converting enzyme, leucine aminopeptidase and carboxypeptidase A. NEP attacked MCH at three sites of the molecule with an apparent affinity of about 12 microM and a kcat. of 4 min-1. The first site of cleavage was at Cys-7-Met-8, i.e. within the peptide loop formed by the internal disulphide bridge. NEP could therefore be considered as an MCH-inactivating peptidase since the degradation products generated are probably devoid of biological activity. In contrast, NEI neither inhibited the degradation of the NEP chromogenic substrate glutaryl-Phe-Ala-Phe-p-aminobenzoate nor was susceptible to proteolysis by NEP. Unlike NEP, angiotensin-converting enzyme, endopeptidase 24.15 and endopeptidase 24.16 appeared totally unable to cleave MCH, whereas the peptide was readily degraded by aminopeptidase M and carboxypeptidase A.
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PMID:Hydrolysis of rat melanin-concentrating hormone by endopeptidase 24.11 (neutral endopeptidase). 152 Feb 71

Using 3-D searching techniques based on algorithms derived from graph theory we have established a striking structural similarity between the structure of bovine carboxypeptidase A and that of the C-terminal domain of bovine leucine aminopeptidase. There is no significant sequence homology between the aminopeptidases and the carboxypeptidases but the strong structural relationship detected in this complex fold suggests that there may be a very remote divergent evolutionary relationship between these two enzyme classes.
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PMID:Three-dimensional structural resemblance between leucine aminopeptidase and carboxypeptidase A revealed by graph-theoretical techniques. 159 16


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