A simplified procedure for measuring amino-procollagen peptidase type I
- 1 June 1979
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 95 (2), 406-412
- https://doi.org/10.1016/0003-2697(79)90747-4
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- A method for assaying the activity of the endopeptidase which excises the nonhelical carboxyterminal extensions from type I procollagenAnalytical Biochemistry, 1978
- Pro—Gln: The procollagen peptidase cleavage site in the α1 (I) chain of dermatosparactic calf skin procollagenFEBS Letters, 1978
- Interaction Between Collagen Type I and Type III in Conditioning Bundles OrganizationConnective Tissue Research, 1977
- Amino-terminal extensions on skin collagen from sheep with a genetic defect in conversion of procollagen into collagenBiochemistry, 1976
- Procollagen peptidase: Its mode of action on the native substrateCell, 1975
- Isolation and characterization of the cyanogen bromide peptides from the α(III)chain of human collagenBiochemistry, 1974
- Chemical properties of the peptide extension in the pα 1 chain of dermatosparactic skin procollagenFEBS Letters, 1972
- Collagen Made of Extended alpha-Chains, Procollagen, in Genetically-Defective Dermatosparaxic CalvesEuropean Journal of Biochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Two Improved and Simplified Methods for the Spectrophotometric Determination of Hydroxyproline.Analytical Chemistry, 1963