Biomedical subjects
Publications and source records attributed to S Hayano.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
To examine the effect of spasmogens on propulsive motility in the intestine, cathartic activity of drugs was investigated. Mice, rats and guinea pigs were individually observed in cages with 20 separate small rooms in which a sheet of filter paper covered the botton of case for observation of feces. The effect was evaluated 1 hr after drug administration. Cathartic activity of spasmogens was the most marked in mice followed by rats, but was rarely observed in guinea pigs. Cholinergic drugs and cholinesterase inhibitors had a cathartic effect in mice and rats, but the activity differed. Drugs such as acetylcholine and physostigmine produced a low cathartic activity even at sublethal and lethal doses. Other drugs as bethanechol, pilocarpine and neostigmine had a dose dependent cathartic effect at doses below lethal ones and were found to be clinically useful for intestinal relaxation after laparotomy. Among autacoids which contract the intestine by direct action on smooth muscles, histamine and bradykinin had no cathartic effect in mice and rats. 5-HT and prostaglandin E2 were dose dependent with a marked cathartic effect in both species. 5-HTP produced the same cathartic activity as that seen with 5-HT in mice, but had no cathartic effect in rats. The cathartic effect of BaCl2 was low, but dose dependent in both species. We recommend this method for the study of the effect of various compounds on the propulsive motility of the intestine.
A method, repetitive counterelectrophoresis (RCE), was devised for detecting specific antibody to streptococcal esterase (STE). Reference antisera were prepared by immunizing rabbits with STE of streptococcal strains as follows: SS379 (group A, type 40), 69882 (group A, type 49), and H36B (group B, type Ib). Some human sera, derived from patients with scarlet fever, were also used as references. By this method, we have confirmed the immunological specificity of the STE produced by strains SS379 (STE-AI), 69882 (STE-AII), H36B (STE-B), and Austin (STE-C, group C) and have shown that the STE produced by strain 10706 (group C) is immunologically identical with STE-AI. Each STE presented a distinct colored line with the respective homologous antibody upon development of enzyme activity except for STE-AII, which formed a round spot with the homologous antibody. Horse activating factor (Hayano and Tanaka, 1973) formed a round spot with each STE. The factor in serum that reacted specifically with STE seemed to correspond to gamma globulin.
Repetitive counterelectrophoresis (RCE), which has been described (Hayano and Tanaka, 1977), was used to assay the contents of antibodies to streptococcal esterases (STE) in sera from patients with scarlet fever. The levels of antibodies to STE were expressed semiquantitatively by reading the intensity of the colored spot developed by RCE with a densitometer. The present study deals with the determination of anti-STE in sera drawn at intervals from 54 patients diagnosed as suffering from scarlet fever. The STE used in this study were prepared from the streptococcal strains as follows. STE-AI was prepared from SS379 (group A, type 40), STE-AII from strain 69882 (group A, type 49), STE-B from strain H36B (group B, lb), and STE-C from strain Austin (group C). Of the 54 cases studied, 32 (59.3%) showed anti-STE-AI, 24 (44.4%) showed anti-STE-AII, 5 (9.3%) showed anti-STE-B, and 23 (42.6%) showed anti-STE-C. Comparison of the titer of anti-streptolysin O (ASLO) with the type of specific reaction of anti-STE-AI and -AII, determined in the same specimen, showed a marked correlation. Of 20 cases giving ASLO titers of 12 or less, 18 showed no sign of anti-STE-AI and -AII and two showed signs of anti-STE-AI. Of 34 cases giving ASLO titers of more than 12, 33 showed signs of anti-STE-AI and/or -AII, 22 showed signs of anti-STE-AI and -AII, 7 showed signs of anti-STE-AI, and 4 showed signs of anti-STE-AII. Of all the cases, 26 showed coincident rises in titers of ASLO and levels of anti-STE-AI and/or -AII during the course of the disease. One case showed the presence of only anti-STE-B. All of the 23 cases that showed the presence of anti-STE-C showed signs of anti-STE-AI. Some of these cases showed a marked increase in levels of anti-STE-C during the course of the disease.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Methods were devised to prepare and estimate quantitatively the extracellular esterases of group A streptococci (STE). Two types of esterase preparations were prepared, corresponding to Stock and Lynn's serotype I (STE I) and II (STE II). The former was prepared from Streptococcus pyogenes strain SS379 (group A, type 40), and the latter from S. pyogenes strain 69882 (group A, type 49). Effects of cupric acetate, sera of various animals, and rabbit antisera to STE I and II on the activities of STE were tested. Cupric acetate added in substrate solution inhibited the activities of STE according to the concentration of cupric acetate. Sera of various animals (calf, guinea pig, horse, sheep, and pig) stimulated the activities of STE and protected them from the inhibitory effect of cupric acetate. Among the sera of various animals, horse serum gave the most potent activating and protecting effect, and was the serum from which the effective factor (horse serum-activating factor, HAF) was extracted by precipitation with ammonium sulfate. STE I was not stimulated by serum or HAF as markedly as STE II, but both enzymes were protected likewise by serum or HAF from the inhibition of cupric acetate. Antibodies to STE I and II were prepared in rabbits. Their effects on STE resembled that of HAF, but differed from the latter in immunological specificity. Activities of STE were stimulated and protected more markedly by homologous antiserum than by heterologous antiserum or normal rabbit serum. Applying suitable conditions, we defined the potency of STE and differentiated antibodies to STE I and II and normal serum quantitatively.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
The occurrence of a streptococcal sialidase (designated St-sialidase) in culture fluids of various streptococci was investigated. St-sialidase was found to occur in strains belonging to groups A, B, C, E, G, H, and L, and the unclassified strains, Streptococcus sanguis and Streptococcus uberis. St-sialidase of group A was confined predominantly to types 4 and 22. St-sialidases, extracted from the culture fluids of some selected strains, were antigenic, eliciting the formation of antibody which effectively neutralized the enzymatic activity of the enzyme. Antisera to the St-sialidases of groups A, B, C, E, G, and L, and Streptococcus sanguis were produced in rabbits. The St-sialidases of groups A, B, and E streptococci were serologically distinct and group-specific. The St-sialidases from groups C, G, and L were serologically homologous, but distinct from St-sialidases of the other groups. Antiserum to the enzyme of strain 10557 (S. sanguis) cross-reacted with the St-sialidase of strain 9927 (S. uberis).
A group of enzymes were prepared from the culture fluids of streptococci belonging to groups A, B, C, G, and L, and from a strain of Streptococcus sanguis. These streptococcal enzymes (designated St-sialidases) released a substance shown to belong to the sialic acid group from the specific substrate BSM-St, a sialomucoid prepared from bovine submaxillary gland. They were inactive on N-acetylneuramin lactose prepared from bovine colustrum and on a sialomucoid prepared from bovine submaxillary mucin, whereas these substances are susceptible to sialidases produced by group K streptococci and by Vibrio cholerae. Some of the St-sialidases were markedly activated by divalent cations, but others showed little response. The heat stability of the enzymes produced by the different strains varied. The optimal pH was between 5.5 and 6.5 with acetate buffer and was about 7 with phosphate buffer. K(m) values were determined for the St-sialidases with BSM-St as substrate.
Explore the source record for details and available documents.