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    CMUR > College of Medicine > School of Medicine > Journal articles >  Item 310903500/30584
    Please use this identifier to cite or link to this item: http://ir.cmu.edu.tw/ir/handle/310903500/30584


    Title: The role of free radicals in the release of noradrenaline from myenteric nerve terminals of guinea-pig ileum
    Authors: Jou, SB;Cheng, JT
    Contributors: 醫學院醫學系神經學科;NATL CHENG KUNG UNIV,COLL MED,DEPT PHARMACOL,TAINAN 70101,TAIWAN;CHINA MED COLL,DEPT NEUROL,TAICHUNG 40421,TAIWAN
    Date: 1997
    Issue Date: 2010-09-24 14:58:11 (UTC+8)
    Publisher: ELSEVIER SCIENCE BV
    Abstract: DNase I of tilapia (Oreochromis mossambicus) was purified to homogeneity. Tilapia DNase I is most active at pH 8.5 with Mg2+ as activator. The Ca2+/Mg2+ pair has a synergistic effect on activation, The enzyme is readily inactivated by heating above 55 degrees C, but is not inactivated by trypsin or 2-mercapto-ethanol under alkaline conditions, with or without CaCl2. Its isoelectric point is 6.0. The 258-amino-acid sequence of tilapia DNase I was derived from overlapping sequences of tryptic, chymotryptic and CNBr peptides, The purified enzyme has two variants differing by a single Lys-->Arg mutation at position 125. The polypeptide chain has one disulfide bridge and one carbohydrate side chain. By mass spectrometry, the purified enzyme shows many molecular mass forms differing by Lys/Arg substitution and sugar-chain length, The major form has a molecular mass of 30914 Da, A 1061-bp nucleotide sequence for the cDNA of tilapia DNase I, obtained by gene cloning and DNA sequencing, contains an ORF coding for a putative 26-residue transmembrane peptide and the mature DNase I polypeptide.
    Relation: JOURNAL OF THE AUTONOMIC NERVOUS SYSTEM 66(3):126-130
    Appears in Collections:[School of Medicine] Journal articles

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