Studies on α2-macroglobulin and trypsin-protein esterase activity
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概要
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1) Fraction-I, which is a portion of serum prtoein separated by means of gel filtration using Sephadx G-200, formed a complex of trypsin-protein esterase (TPE) when treated with trypsin and did not lose its enzymatic activity. Mild anti-tryptic activity was also demonstrated in this fraction.The ratio of the tryptic activity to the anti-tryptic activity was 5. It is considered that the existence of anti-tryptic activity is due to a loss of enzymatic activity caused by the formation of the complex.2) The esterase activity of α2M-enzyme complex in serum was studied with the use of α-N-benzoyl-DL-arginine-p-nitroanilid HCl (BAPNA) as the synthesized substrate in human subjects. It was found that the serum protein, which had esterase activity, could be absorbed by anti-α2M rabbit serum immunochemically. This complex could also protect trypsin esterase activity from soybean trypsin inhibitor. Moreover, our data suggested that one mole of α2M was bound to two moles o trypsin.3) In 83 patients with various diseases, the values of serum TPE activity were compared with those of serum α2M measured by an immunological method. The result, that the correlation coefficient between the two values was 0.95 showed the greatly significant relation of TPE activity to α2M level in serum. Accordingly, the measurement of α2M concentration in serum can be replaced by the determination of serum TPE activity, which is a simpler technique.
- 日本電気泳動学会の論文
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