Catalytic activity and thermostability of dehydrogenase conjugates with cortisol and progesterone.
The conjugates of glucose-6-phosphate dehydrogenase, lactate dehydrogenase, and malate dehydrogenase with progesterone and cortisol, containing 1-40 steroid molecules per enzyme molecule, were obtained by the reactions of N-succinimide esters of the 3-[O-(carboxymethyl)oximes)] of cortisol and progesterone with a protein in a water-DMFA (10%) medium. The catalytic activity and thermostability of dehydrogenases and their steroid conjugates were kinetically studied. The effects of the modification degree on the activity and thermostability of dehydrogenases by their hydrophobization were studied and discussed. Practical recommendations for using the dehydrogenase-steroid conjugates in enzyme immunoassay are given.
Metelitza
D I
DI
Institute of Bioorganic Chemistry, BSSR Academy of Sciences, Minsk, U.S.S.R.
Eryomin
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AN
Karasyova
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EI
Markina
V L
VL
D002384:Catalysis; D004789:Enzyme Activation; D004795:Enzyme Stability; D005954:Glucosephosphate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D006358:Hot Temperature; D006854:Hydrocortisone / Q000737:chemistry*; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D008291:Malate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D011374:Progesterone / Q000737:chemistry*; D013816:Thermodynamics
D011374:Progesterone; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D006854:Hydrocortisone