Release of lysosomal acid hydrolases from dog cardiac muscle after cell damage may precede final cellular destruction. An in vivo experiment was designed to study the effects of acute myocardial ischemia on the integrity of the lysosomal particles. The left coronary artery was ligated and the animals were sacrificed at 2, 6, 24, and48 hrs. Aliquots were homogenized and separated by ultracentrifugation into supernatant (S-fraction), large granule (L-fraction) and nuclear fraction (N-fraction).
Sequential arterial and coronary sinus samples, the total homogenate and its fractions (S, L and N) were assayed for the activities of cathepsin (3.4.4.23), β-glucuronidase (3.2.1.31), acid phosphatase (3.1.3.2) and cytochrome oxidase (1.9.3.1). There was a steady fall in total homogenate activity for these enzymes within 2 hrs, and the activities reached into half of intact right ventricle in the same heart at 48 hrs.
Cathepsin, acid phosphatase and cytochrome oxidase activity decreased in all fractions except the S-fraction of cytochrome oxidase. The latter was the only fraction in which the activity increased after ischemia.
Serum acid hydrolases, GOT and LDH titers remained elevated and varied reciprocally with their concentration in total homogenate and especially in S-fraction.
The study demonstrates myocardial lysosomal and mitochondrial enzyme activity which is complex and selective retention of enzymes.
Finally we demonstrated that the same situation in serum enzyme activities of human acute myocardial infarct, and that emphasized an importance of the knowledge of lysosomal concept concerning with ischemia and cell damage from a point of clinical pathology.

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Precipitin specifically reacted with saline extract from cancer tissue of human stomach and colon was produced in rabbit sera immunized with extract of gastric cancer. Cancer specific precipitation reaction was demonstrated by ring test with anti-gastric cancer immune rabbit serum absorbed with pooled human plasma and extracts of normal gastric linings. The reaction was inhibited by glucosamine and galactosamine as simple sugars and urine from gastric cancer patients, but not inhibited by extracts from fetal stomach, liver, intestine and kidney. Single precipitin band was observed in agar gel and immuno-electrophoresis between extract of gastric cancer and IgG fraction of anti-gastric cancer rabbit serum.
Purified antigenic substance was prepared by alcohol precipitation of saline extract of gastric cancer tissue followed by DEAE-cellulose colmn chromatography and polyacrylamide gel electrophoresis. From the chemical examination, main component of the antigenic substance proved to be a protein. The antigenic activity was lost by the action of pepsin and pronase.

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Oligosaccharides showing heterophile red cell antigenicity were isolated from the partial hydrolysate of purified lipopolysaccharide of S-form Shigella dysenteriae. An oligosaccharide sh-2 was disaccharide composed of galactose. The results of alkaline degradation, periodate oxidation, gaschromatographic analysis of permethylated substance and enzymatic treatment indicated that the structure of sh-2 was probably β-D-Gal- (1→2) -D-Gal. Another oligosaccharide sh-12 was a tetrasaccharide containing galactose and rhamnose in a molar ratio of 1 : 1. The probable structure of sh-12 was β-D-Gal- (1→2) -D-Gal- (Rha, Rha) from the results of enzymatic degradation and its high immunological activity.
The structural relationship between human blood group substance and the heterophile antigen of Shigella dysenteriae was discussed on the immunological specifity of human red cell antibody present in anti- Shigella dysenteriae immune chiken serum.

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