{"database":"biostudies-other","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["201(1)"],"submitter":["Puistola U"],"journal":["The Biochemical journal"],"pagination":["215-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1163628"],"abstract":["Crude preparations of lysyl hydroxylase were extracted from chick-embryo tendons synthesizing exclusively type I collagen, chick-embryo sterna synthesizing exclusively type II collagen and HT-1080 sarcoma cells synthesizing exclusively type IV collagen. No differences were found in the Km values for Fe2+, 2-oxoglutarate and ascorbate between these three enzymes preparations. Similarly no differences were found in the Km values for type I and type II protocollagens and the rate at which type IV protocollagen is hydroxylated between these enzyme preparations. The extent to which type I protocollagen could be hydroxylated by the three enzymes was likewise identical. These data strongly argue against the existence of collagen-type-specific lysyl hydroxylase isoenzymes."],"repository":["biostudies-other"],"data_source":["Europe PMC"],"pubmed_authors":["Puistola U"],"additional_accession":[]},"is_claimable":false,"name":"Catalytic properties of lysyl hydroxylase from cells synthesizing genetically different collagen types.","description":"Crude preparations of lysyl hydroxylase were extracted from chick-embryo tendons synthesizing exclusively type I collagen, chick-embryo sterna synthesizing exclusively type II collagen and HT-1080 sarcoma cells synthesizing exclusively type IV collagen. No differences were found in the Km values for Fe2+, 2-oxoglutarate and ascorbate between these three enzymes preparations. Similarly no differences were found in the Km values for type I and type II protocollagens and the rate at which type IV protocollagen is hydroxylated between these enzyme preparations. The extent to which type I protocollagen could be hydroxylated by the three enzymes was likewise identical. These data strongly argue against the existence of collagen-type-specific lysyl hydroxylase isoenzymes.","dates":{"release":"1982-01-01T00:00:00Z","publication":"1982 Jan","modification":"2019-08-04T07:22:18Z","creation":"2019-08-04T07:22:18Z"},"accession":"S-EPMC1163628","cross_references":{"DOI":["10.1042/bj2010215 "]}}