Detail of "4313-73-9"

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Enkephalin diazomethyl and chloromethyl ketones: synthesis and biological activity

Enkephalin diazomethyl and chloromethyl ketones: synthesis and biological activity. Medzihradszky, K.; Szecsi, J.; Csanady, G.; Hepp, J. (Cent. Res. Inst. Chem., Hung. Acad. Sci., Budapest H-1025, Hung.). Pept., Proc. Eur. Pept. Symp., 17th, Meeting Date 1982, 623-8. Edited by: Blaha, Karel; Malon, Petr. de Gruyter: Berlin, Fed. Rep. Ger. (English) 1983. CODEN: 50GFAA. DOCUMENT TYPE: Conference CA Section: 34 (Amino Acids, Peptides, and Proteins) Section cross-reference(s): 1 Enkephalin chloromethyl ketones H-Tyr-X-Gly-Phe-Leu-CH2Cl (I; X = Gly, D-Ala) were prepd. by coupling Boc-Tyr-X-Gly-OH (Boc = Me3CO2C) with H-Phe-Leu-CH2Cl (II) and Boc-deblocking the resulting Boc-Tyr-X-Gly-Phe-Leu-CH2Cl, whereas enkephalin diazomethyl ketones H-Tyr-X-Gly-Phe-Leu-CH2N2 (X = Gly, D-Ala) were prepd. by coupling Msoc-Tyr-X-Gly-OH with H-Phe-Leu-CH2N2 (III) and deblocking the resulting Msoc-Tyr-X-Gly-Phe-Leu-CH2N2. Z-Phe-Leu-OH (Z = PhCH2O2C) was treated with CH2N2 by the mixed anhydride method to give Z-Phe-Leu-CH2N2, which was treated with HCl to give Z-Phe-Leu-CH2Cl, which was Z-deblocked by HBr/HOAc to give II. Pht-Phe-Leu-OH (Pht = phthaloyl) was converted to Pht-Phe-Leu-CH2N2, which was Pht-deblocked by hydrazinolysis to give III.In this experiment, several chemicals are used like 4313-73-9 and 77180-21-3 The activity of I (X = Gly) on guinea pig ileum is 5 times greater than that of [Leu5]-enkephalin, whereas the activity of I (X = Gly) on mouse vas deferens is only one tenth that of the natural peptide. The binding of I (X = D-Ala) to opiate receptors of rat brain membrane prepns. are discussed. .

Purification and characterization of a developmentally regulated carboxypeptidase from Mucor racemosus

Purification and characterization of a developmentally regulated carboxypeptidase from Mucor racemosus. DiSanto, Michael E.; Li, Quanzhi; Logan, David A. (Dep. Biosci. Biotechnol., Drexel Univ., Philadelphia, PA 19104, USA). J. Bacteriol., 174(2), 447-55 (English) 1992. CODEN: JOBAAY. ISSN: 0021-9193. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Section cross-reference(s): 10 A developmentally regulated carboxypeptidase was purified from hyphae of the dimorphic fungus Mucor racemosus. The enzyme, designated carboxypeptidase 3 (CP3), has been purified greater than 900-fold to homogeneity and characterized. The carboxypeptidase migrated as a single electrophoretic band in isoelec. focusing polyacrylamide gel electrophoresis, with an isoelec. point of pH 4.4. The apparent mol. mass of the native enzyme was estd. by gel filtration to be 52 kDa. SDS-PAGE under nonreducing conditions revealed the presence of a single polypeptide of 51 kDa.Several substances with their cas registry numbers 9031-98-5 and 4313-73-9 may be metioned in this study. SDS-PAGE of CP3 reacted with 2-mercaptoethanol revealed the presence of two polypeptides of 31 and 18 kDa, indicating a dimer structure (a1b1) of the enzyme with disulfide-linked subunits. By using [1,3-3H]diisopropylfluorophosphate as an active-site labeling reagent, it was detd. that the catalytic site resides on the small subunit of the carboxypeptidase. With N-carboben zoxy-L-phenylalanyl-L-leucine (N-CBZ-Phe-Leu) as the substrate, the Km, kcat, and Vmax values were 1.7 ′ 10-4 M, 490 s-1, and 588 mmol of Leu released per min per mg of protein, resp. CP3 was detd. to be a serine protease, since its catalytic activity was blocked by the serine protease inhibitors diisopropylfluorophosphate, phenylmethylsulfonyl fluoride, and 3,4-dichloroi Socoumarin (DCI). The enzyme was strongly inhibited by the mercurial compd. p-chloromercuribenzoate. The carboxypeptidase readily hydrolyzed peptides with aliph. or arom. side chains, whereas most of the peptides which contained glycine in the penultimate position did not serve as substrates for the enzyme. Although CP3 activity was undetectable in Mucor yeast cells, antisera revealed the presence of the enzyme in the yeast form of the fungus. The partial amino acid sequence of the carboxypeptidase was detd. .