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dc.contributor.authorSu, Wen-Jin
dc.contributor.author苏文金
dc.contributor.authorWu, Guo-Ping
dc.contributor.authorCao, Min-Jie(Biol Engn, Xiamen)
dc.contributor.authorLiu, Bing-Xin(Biol Engn, Xiamen)
dc.contributor.authorChen, Yan(Jimei Univ)
dc.date.accessioned2011-07-31T04:12:36Z
dc.date.available2011-07-31T04:12:36Z
dc.date.issued2008
dc.identifier.citationJ. Agric. Food Chem., 2008, 56 (20), pp 9653–9660zh_CN
dc.identifier.issn0021-8561
dc.identifier.urihttp://dx.doi.org/doi:10.1021/jf801477r
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10336
dc.description.abstractA leucine aminopeptidase was purified for the first time from marine fish red sea bream (Pagrus major skeletal muscle to homogeneity with 4850-fold and a yield of 7.4%. The purification procedure consisted of ammonium sulfate fractionation and chromatographies including DEAE-Sephacel, Sephacryl S-200, hydroxyapatite, and phenyl-Sepharose. The enzyme was approximately 96 kDa as estimated by SIDS-PAGE and gel filtration and preferentially hydrolyzed substrate Leu-MCA. The enzymatic activity was optimal at 45 degrees C and pH 7.5. The K-m and k(cat) values of the enzyme for Leu-MCA were 1,55 mu M and 26.4 S-1 at 37 degrees C, respectively. Activation energy (E-a) of the enzyme was 59.6 kJ M-1. The enzyme was specifically inhibited by metal-chelating agents, and Zn2+ and (or) Mn2+ seemed to be its metal cofactor(s). In addition, bestatin strongly inhibited its activity, and K-i was 1.44 mu M. Using a highly specific polyclonal antibody, the location of enzyme was demonstrated intracellularly and distributed in different tissues.zh_CN
dc.description.sponsorshipNational Natural Scientific Foundation of China [30571450]; Natural Scientific Foundation of Fujian Province [2006J0368]; Foundation for Innovative Research Team of Jimei University [2006A002]zh_CN
dc.language.isoenzh_CN
dc.publisherAMER CHEMICAL SOCzh_CN
dc.subjectRed sea breamzh_CN
dc.subjectleucine aminopeptidasezh_CN
dc.subjectpurificationzh_CN
dc.subjectcharacterizationzh_CN
dc.subjectWestern blotzh_CN
dc.titleLeucine Aminopeptidase from Red Sea Bream (Pagrus major) Skeletal Muscle: Purification, Characterization, Cellular Location, and Tissue Distributionzh_CN
dc.typeArticlezh_CN


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