Publication | Open Access
Protein disulphide-isomerase activity in chick-embryo tissues. Correlation with the biosynthesis of procollagen
31
Citations
10
References
1980
Year
Animal PhysiologyChick-embryo TissuesEmbryologyBiosynthesisDevelopmental BiologyProtein ExpressionBiochemistryProtein Disulphide-isomerase ActivityMedicineNatural SciencesCellular EnzymologyProtein BiosynthesisMaximal Procollagen SynthesisEmbryonic DevelopmentProteomicsEnzymatic ModificationPoultry ScienceProcollagen Synthesis
Protein disulphide-isomerase activity was determined in homogenates of chick-embryo tissues. Activities were highest in tissues active in procollagen synthesis and were maximal at the developmental stage of maximal procollagen synthesis. These variations in protein disulphide-isomerase activity correlate closely with those previously observed for protocollagen hydroxylase activities.
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