ISSN:
0173-0835
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Improved separation of alpha chains of collagen type I (α1[I]2 α2[I]), type III(α1[III]3), and type V(α1[V] α2[V]α3[V]) was achieved by noninterrupted sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a negatively charged reducer, thioglycolic acid. The thioglycolic acid, added to the running buffer of the cathodic reservoir, in the middle of electrophoresis quickly migrated in the gel anode, reducing interchain disulfide linkages in collagen type III and dissociating it into its alpha chain monomer, α1[III], without an interruption of electrophoresis. The alpha chain, α1[III], migrated more slowly than the α1[I] and α2[I] chains of collagen type I, resulting in an excellent separation of α1[III] from α1[I]. The mobility of α1[III] could be controlled by varying the time of thioglycolic acid addition to the running buffer. This enabled us not only to separate α1[III] from α1 [I] and α1[V], but also to precisely quantitate these alpha chains, even at low protein loading of mixed samples.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.1150100108
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