Purification and enzymatic properties of lysyl hydroxylase from fetal porcine skin.
Biochemistry, 1979/12/25;18(26):5828-32.
PMID: 117833
Impact factor: 3.321
Abstract
Lysyl hydroxylase from fetal porcine skin is shown to bind in a highly specific manner to aminoethyl-Sepharose 4B. When coupled to ammonium sulfate fractionation and DEAE-cellulose chromatography, chromatography of lysyl hydroxylase preparations on aminoethyl-Sepharose 4B has yielded a highly purified (greater than 95%) preparation of lysyl hydroxylase. The enzyme consists of two subunits with molecular weights of 70 000 and 115 000. The overall recovery of activity was 2.5%, yielding approximately to 3.5 mg of purified enzyme from 900 g of fetal porcine skin. The enzyme is more active at 30 degrees C than at 37 degrees C and has a pH optimum near 8.0. Both catalase and bovine serum albumin are required by the enzyme for maximum activity. The sulfhydryl reagents p-(chloromercuri)-benzoate, N-ethylmaleimide, and iodoacetamide are potent inhibitors of the enzyme, whereas dithiothreitol appears to be an activator.
MeSH terms
Animals; Dithiothreitol; Female; Fetus; Kinetics; Mixed Function Oxygenases; Pregnancy; Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase; Skin; Sulfhydryl Reagents; Swine
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