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- W3141781142 abstract "We used bovine cornea as starting material, pepsin treatment in acetic acid solution to extract the mixture of typeⅠandⅤcollagens, and salt precipitation and dialysis to purify and isolate each type of the collagens. The preparation was analyzed using sodium dodecyl sulphate polyacrylamide gel electrophoresis. 2-mercaptoethanol used as reducing agent cut off the disulfide bonds, which was utilized to analyze the structure of disulfide bonds involved betweenαchains in some types of collagens. At the same time, we discovered that the structure of disulfide bonds amongαchains potentially existed in the typeⅤcollagen prepared from the pepsin-treatment extraction at 4℃. Through quantitative analysis, we obtained that, compared with those pepsin-treated at 4℃, the relative molecular weights ofα1(Ⅴ) andα2(Ⅴ) subunits pepsin-treated at room temperature decreased by 4.6% and 6.0%, respectively. It is concluded that typeⅤcollagen can be prepared from bovine cornea by use of pepsin treatment, salt precipitation and dialysis. The interchain and/or intermolecular disulfide bonds potentially lie near the edges of termini of typeⅤcollagen molecules existing in extracellular matrix, and there are few of the intermolecular and/or intramolecular crosslinks formed by lysine or hydroxylysine or histidine residues in typeⅤcollagen." @default.
- W3141781142 created "2021-04-13" @default.
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- W3141781142 date "2011-01-01" @default.
- W3141781142 modified "2023-09-26" @default.
- W3141781142 title "Extraction of TypeVCollagen From Bovine Cornea and Its Structural Analysis" @default.
- W3141781142 hasPublicationYear "2011" @default.
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