著者

TSUNEO SUZUKI SEIICHI KASHIMURA KAZUO UMETSU

出版者

Tohoku University Medical Press

雑誌

The Tohoku Journal of Experimental Medicine (ISSN:00408727)

巻号頁・発行日

vol.124, no.3, pp.267-275, 1978 (Released:2008-11-28)

参考文献数

23

被引用文献数

1

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LDH and GOT isozyme patterns in the heart muscle of forensic pathological cases were investigated to find out the relationship between their changes and the causes of death. In most cases of death by violence, natural causes, poisoning and cold, the sum of LDH-1 and LDH-2 averaged about 80-90% of the total LDH, and GOTs was equal to or slightly lower than GOTm. In about two thirds of cases of asphyxia and drowning, LDH-1 and LDH-2 decreased and LDH-3, LDH-4 and LDH-5 increased. The activity of GOTs decreased and the ratio of GOTs/GOTm diminished. In neonate, LDH-3 showed the highest activity, followed by LDH-2 and LDH-1. GOTm was much less than GOTs. In most cases of cardiac death from unknown cause and cot death, LDH-3 increased remarkably, though it was less than LDH-1 and LDH-2, and GOTm became much less than GOTs. These findings revealed that there were some similarities in the LDH and GOT isozyme patterns in the heart muscle of the cardiac death from unknown cause and cot death and that of neonate.

著者

Kazuo UMETSU Suezo KOSAKA Tsuneo SUZUKI

出版者

The Japanese Biochemical Society

雑誌

The Journal of Biochemistry (ISSN:0021924X)

巻号頁・発行日

vol.95, no.1, pp.239-245, 1984 (Released:2008-11-18)

参考文献数

20

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A lectin was purified from the hemolymph of Allomyrina dichotoma larvae by affinity chromatography on acid-treated Sepharose 4 B. The purified lectin showed two protein bands on polyacrylamide gel electrophoresis. These two lectin bands (allo A-I and -II) were separated by DEAE-Cellulofine column chromatography. By gel filtration on Sephadex G-100, the molecular weights of alto A-I and -II were estimated to be 65, 000 and 66, 500, respectively. On the other hand, by SDS-polyacrylamide gel electrophoresis after cross-linking of subunits with glutaraldehyde, they are estimated to be 38, 000 and 39, 000, respectively. On SDS-polyacrylamide gel electrophoresis, it was proved that both allo A-I and -II lectin consisted of two subunits, respectively. The molecular weights were 17, 500 and 20, 000 for allo A-I, and 19, 000 and 20, 000 for allo A-II. The isoelectric points of alto A-I and -II were estimated to be 6.4 and 5.9, respectively. On double immunodiffusion, allo A-I and -II gave single precipitin lines, which fused completely with each other, against the antibody to crude allo A. The hemag-glutinating activity of allo A-I and -II was inhibited only by β-linked D-galactose such as lactose and lactulose.