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• W2235779568 abstract "At 24 h after injection of 16-day chick embryos with [C-3H]pyridoxine hydrochloride, some of this label appears in the epiphysial cartilage. Over 35% of this radioactivity appears in the form of [G-3H]pyridoxal and a further 30% as other vitamin B-6 compounds. Partial purification of lysyl oxidase from the labelled epiphysial cartilage reveals a single peak of radioactivity coinciding with a single peak of enzyme activity. On dialysis against phosphate-buffered saline, 75% of this radioactivity is found to be non-diffusible. After incubation with isonicotinic acid hydrazide, a carbonyl reagent that appears to inhibit lysyl oxidase both in vivo and in vitro, a further 70% of the radioactivity is lost, with a roughly corresponding loss of enzyme activity. It is suggested that a form of vitamin B-6 is required as a cofactor of lysyl oxidase, and that this may have important implications in terms of connective-tissue metabolism." @default.
• W2235779568 created "2016-06-24" @default.
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• W2235779568 date "1977-11-01" @default.
• W2235779568 modified "2023-09-27" @default.
• W2235779568 title "Evidence for the role of vitamin B-6 as a cofactor of lysyl oxidase" @default.
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• W2235779568 doi "https://doi.org/10.1042/bj1670463" @default.
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