Liver alcohol dehydrogenase subunit equivalence studied by rapid sampling of alcohol product formed from sequentially bound [4alpha-3H]NADH. |
| |
Authors: | R J Kordal S M Parsons |
| |
Institution: | 1. Orthopaedic Research Laboratories, Department of Orthopaedic Surgery, University of the Witwatersrand, Johannesburg, South Africa;2. Department of Medical Biochemistry, University of Cape Town, Cape Town, South Africa |
| |
Abstract: | Proteoglycans of calf and steer articular cartilage were studied with a view of assessing structure and changes occurring as a result of the aging process. The average reduction in hydrodynamic size noted in steer was associated with a diminution in size of the chondroitin sulfate-rich region of the core protein as well as the chondroitin sulfate chains themselves. By contrast the keratan sulfate-rich region was hydrodynamically larger in steer although the keratan sulfate chains were only slightly longer than in calf. The proteoglycans showed a maturation-related decrease in chondroitin sulfate content (shorter chains, fewer chains, smaller chondroitin sulfate-rich region) and an enrichment in keratan sulfate chains in both the chondroitin sulfate-rich and keratan sulfate-rich regions. Proteoglycans from both age groups contained an oligosaccharide which was recovered mainly from outside of the keratan sulfate-rich region. There were no significant differences in size between keratan sulfate chains recovered from the keratan sulfate-rich region and the chondroitin sulfate-rich region. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|