PROTEIN METABOLISM IN REGENERATING WOUND TISSUE FUNCTION OF THE SULFUR AMINO ACIDS.
Abstract
A technique was developed which could be used to differentiate between cystine incorporated into non-collagenous proteins by peptide bonds and that which is associated with the protein by disulfide bonds only. The method depends on the irreversible conversion of disulfide and sulfhydryl groups into thiosulfate derivatives with the simultaneous separation of the protein from the non-protein thiosulfates by dialysis. Using this method with cystine-S35, it was possible to follow the rate of protein synthesis and at the same time the rate of metabolic utilization of these proteins by the wound tissue cells. The cells in wound tissue at different stages of regeneration were separated into nuclear, mitochondrial, microsomal and nonparticulate fractions by differential centrifugation. The metabolism of cystine bound by the above types of bond to the proteins of these fractions was investigated. The period of most active cell protein and collagen formation could be identified. Preliminary steps for isolating the enzyme systems involved in these processes were undertaken. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 15, 1965
- Accession Number
- AD0466579
Entities
People
- Martin B. Williamson
Organizations
- Loyola University Chicago