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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46555

Title: Proteolysis of Actomyosin by Cathepsins B, L, L-like, and X from Mackerel (Scomber australasicus)
Authors: Shann-Tzong Jiang
Jai-Jaan Lee
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: seafood
cathepsins
Mackerel
actomyosin
proteolysis
Date: 1996
Issue Date: 2018-05-23T06:19:00Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract: Cathepsins B and L and cathepsin L-like proteinase degraded myosin heavy chain of actomyosin (AM) into several fragments with molecular masses (MW) of 154, 146, 138, 67, and 36 kDa; 164 and 155 kDa; and 135, 128, and 69 kDa, respectively. In the presence of 0.6 M NaCl, however, the MHC was degraded by cathepsin L into 164, 155, 41, and 37 kDa fragments. The hydrolytic rate of these three proteinases on AM was faster at pH 5.0 than at pH 6.0. Actin seemed to be resistant against hydrolysis by cathepsins B, L, and L-like in the absence of 0.6 M NaCl. According to SDS−PAGE analysis, cathepsin X, a novel cysteine proteinase, did not degrade AM.
Relation: 44(3) pp.769–773
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46555
Appears in Collections:[食品科學系] 期刊論文

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