Isolation and characterization of type III collagen from bovine cardiac muscle |
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| Affiliation: | 1. Istituto di Biomedicina e Immunologia Molecolare (IBIM), Consiglio Nazionale Delle Ricerche, Via U. La Malfa 153, 90146 Palermo, Italy;2. Dipartimento dell''Innovazione Industriale e Digitale (DIID), Università di Palermo, Viale delle Scienze, Edificio 6, 90128 Palermo, Italy;3. Dipartimento di Scienze e Tecnologie Biologiche, Chimiche e Farmaceutiche (STEBICEF), Università di Palermo, Viale delle Scienze, Edificio 16, 90128 Palermo, Italy;4. Istituto di Biofisica (IBF), Consiglio Nazionale Delle Ricerche, Via U. La Malfa 153, 90146 Palermo, Italy |
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| Abstract: | ![]()
- 1.1. Bovine cardiac muscle collagen was solubilized by limited digestion with pepsin and subsequently fractionated by differential salt precipitation.
- 2.2. Chromatographie studies on CM-cellulose and agarose of pepsin-soluble collagen and its salt-precipitated fractions showed it to be composed of type I collagen and a species with a mol. wt of 285,000 daltons, having an amino acid composition characteristic of type III collagen.
- 3.3. The molecular structure of the 285,000-dalton component was confirmed as [α1(III)]3 after reduction with dithiothreitol to a chains having the same amino acid composition.
- 4.4. Cyanogen bromide peptides of pepsin-soluble collagen which co-eluted on CM-cellulose and were identified as α1(I)-CB8 and α1(III)-CB8 showed a molar ratio of 2:1 indicating that 25% of the collagen molecules solubilized are [α1(III)]3.
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