Studies relating to the interactions of proteins with hormones, metabolites and drugs in biological systems
Degree GrantorUniversity of Canterbury
Degree NameDoctor of Philosophy
The methods used to study the interaction of small ions and, molecules with the serum proteins, including both the experimental technique and the analysis of data, have been reviewed. Electrophoresis on graded poly-acrylamide gel was use to study the interactions of more than eight compounds with 15-20 electrophoretically distinguishable fractions of human serum protein. Those found to interact were aluminium sulphate, calcium chloride, sodium acetate, 5-aminocridine, sodium barbitone, sodium butyrate, caffeine, chloromycetin, chlorpheniramine maleante, sodium citrate, codeine phosphate, dexamphetamine sulphate, dihydrotretomycin sulphate, ephedrine hydrochloride, hexamethonium bromide, isorenaline sulphate, sodium lactate, L-methionine, methylamine, naphazoline nitrate, phenazone, phenoxymethyl penicillin, phenylephrine hydrochloride, physostigmine sulphate, sodium phytate, sodium pyruvate, sodium saccharin, streptomycin sulphate, sodium urate, urethane, sodium stearate, and L-tyrosine. A protein fraction not dound in the electrophetic pattern of fresh serum appeared after dialysis against a low ionic-strength buffer for a day, or after storage at room temperature for a day, or at 1°C. for about eight days. It did not appear after 22 days at -15°C. and only a little formed after eight days of dialysis against high ionic strength buffer (higher than 0.16M). Heating serum at 37°C. for four hours produced only a little of this fraction. The electropheric patterns of the folloing Cohn fractions of human serum have been determined: α-globulin (fraction IV-1), β-globulin (IV-4), α₁-lipoprotein (IV-5), α₂-mucoprotein (IV-6), β₁-metal combining protein (IV-7), α-glycoprotein (VI-1a), α-glycoprotein (VI-1b), and caeruloplasmin.