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Biomedical subjects

T Takagi

Publications and source records attributed to T Takagi.

At least 937 records · Page 52Linked to original sources

Chenodeoxycholic acid-induced diarrhea in rats: effects of atropine and codeine.

Orally administered chenodeoxycholic acid (300 mg/kg) produced diarrhea and accumulation of gastro-intestinal fluid in rats. The fluid in the stomach and small intestine remained accumulated even after the accumulated colonic fluid and the diarrheal excretion decreased. When instilled into an intestinal closed-loop, chenodeoxycholic acid caused a marked inhibition of fluid absorption in the colon and jejunum but less effect in the ileum. On the contrary, an intravenous administration of chenodeoxycholic acid caused neither diarrhea nor impairment of colonic absorption of fluid. Atropine and codeine (10 mg/kg s.c.) blocked or at least delayed the diarrhea produced by oral administration of chenodeoxycholic acid. The antidiarrheal activity of codeine was found to be more potent and longer-lasting than that of atropine. Both drugs delayed the passage of chenodeoxycholic acid containing gastric fluid into the duodenum, but neither of them prevented chenodeoxycholic acid-induced jejunal secretion of fluid and electrolytes. These results indicate that the diarrheal excretion by chenodeoxycholic acid was ascribable to the impairment of fluid absorption in the colonic mucosa and partly to the activation of gastro-intestinal propulsive motility.

Analgesia↗

Amino acid sequence of chicken fibrinopeptide A.

Chicken fibrinopeptide A was isolated and the complete amino acid sequence was established. It is a pentadecapeptide with the sequence of Gln(Pyr)-Asp-Gly-Lys-Thr-Thr-Phe-Glu-Lys-Glu-Gly-Gly-Gly-Gly-Arg and is homologous with mammalian fibrinopeptide A. Two peptides which appear to be derivatives of fibrinopeptide A were also isolated. One of these appeared to be fibrinopeptide A with NH2-terminal pyroglutamic acid; the other was fibrinopeptide A which lacked the COOH-terminal arginine residue.

Amino Acid Sequence↗

Amino acid sequence of the beta chain of human fibrinogen: homology with the gamma chain.

The beta chain of human fibrinogen is composed of 452 +/- 5 amino acid residues, 14 of which are methionines. Consistent with these findings we have isolated and characterized 15 fragments after cyanogen bromide digestion of carboxymethylated beta chains. The arrangement of several of these peptides was deduced on the basis of overlapping peptides isolated from the fragments D and E produced by the plasmic digestion of fibrinogen and/or from a tryptic digest of citraconylated beta chains. Most of the other cyanogen bromide fragments can be aligned by homology with the alpha and/or gamma chains from human fibrinogen, although the positioning of a few of the smallest peptides is still ambiguous. The homology of the beta chain with the gamma chain is especially strong in certain regions of the domain that includes fragment D.

Amino Acid Sequence↗

Isolation of a membrane protein from R rubrum chromatophores and its abnormal behavior in SDS-polyacrylamide gel electrophoresis due to a high binding capacity for SDS.

A membrane protein insoluble in water was isolated by gel chromatography in the presence of 0.1% sodium dodecyl sulfate (SDS) from chromatophores of a photosynthetic bacterium, Rhodospirillum rubrum. This is one of the major membrane proteins of the chromatophore. The protein was found to bind about four grams of SDS per gram, a value which is more than twice the amount generally observed with protein polypeptides derived from water-soluble globular proteins. The electrophoretic behavior of the complex between the membrane protein and SDS is abnormal due to this high capacity for binding SDS. Estimation of the molecular weight of this protein by SDS-polyacrylamide gel electrophoresis was thus impossible. Such an anomaly in SDS binding is unlikely to be restricted to the particular membrane protein described in this paper. The possibility of such a deviation from standard behavior in the interaction with SDS should be taken into consideration in studies of other membrane proteins, since SDS is often used both in analytical and preparative procedures.

Bacterial Chromatophores↗

Construction of an L-arginine-producing mutant in Serratia marcescens. Use of the wide substrate specificity of acetylornithinase.

L-Arginine biosynthesis in Serratia marcescens Sr41 was found to be controlled by (a) feedback inhibition of N-acetylglutamate synthetase and (b) repression of some L-arginine biosynthetic enzymes, and an L-arginine-degrading system was found to exist. Accordingly, an L-arginine-producing mutant (aru argR argA) of S. marcescens Sr41 was constructed as follows. A mutant incapable of L-arginine utilization (aru) was obtained from the wild strain. Subsequently, from the lysine auxotroph (lysA) of aru mutant, a mutant having derepressed L-arginine biosynthetic enzymes (argR) was isolated by screening for colonies that could utilize Nalpha-acetyl-L-lysine in the presence of L-arginine. This selection was based on the finding that acetylornithinase of S. marcescens hydrolyzed Nalpha-acetyl-L-lysine. On the other hand, to obtain a mutant with feedback-resistant N-acetylglutamate synthetase (argA), the proAB argD argR triple mutant was isolated from the indirectly suppressed revertant (proAB argD) of the proline auxotroph (proAB). Next, the argA mutant was isolated from the triple mutant by selection for resistance to 3,4-dehydro-DL-proline in the presence of L-arginine. The argA mutation was introduced into the aru lysA argR strain by PS20-mediated cotransduction with lysA+. The aru argR argA lysA+ transductant produced 25 mg/ml of L-arginine in the medium.

Acetyl Coenzyme A↗

Pathological studies on atrioventricular conduction disturbances.

A histopathological study was made on 150 autopsied hearts according to the method of Lev in order to investigate the correlation of conduction disturbances with the branching pattern of the bundle branches. Subsequently, the study of bundle branch block and A-V block cases revealed that no explicit correlation existed between histopathological changes and functional disturbances nor between disturbances in conduction (i.e. breakdown of the physiological mechanism) and histopathological findings.

Adolescent↗

Construction of a urocanic acid-producing strain of Serratia marcescens by transduction.

In Serratia marcescens, the mutation responsible for triazolealanine (TRA) resistance was transferred from a TRA-resistant mutant to a urocanase-less mutant by PS20-mediated transduction. The two crosses were performed using as donors two TRA-resistant mutants, whose phenotypes included increased levels of histidine-biosynthetic enzymes and feedback-insensitive phosphoribosyltransferase. In one cross, TRA-resistant transductants were urocanase-less mutants having only increased levels of the enzymes and barely detectable levels of urocanic acid. In the other cross, the transductants were urocanase-less mutants having both phenotypes of the donor, and most produced high concentrations (10.5 mg/ml) of urocanic acid.

Alanine↗

Extradural hemorrhage in the newborn as a result of birth trauma.

During the past 18 years, 134 autopsies of intracranial hemorrhages were performed in the Department of Pathology, and 2 cases of extradural hemorrhages were discovered (2.2%). 5 cases of extradural hemorrhage (2 of our own treated surgically and 3 untreated found at autopsy) are described in detail. 1 of the 2 cases treated surgically responded favorably to surgical treatment. The mechanism of hemorrhage into extradural spaces is investigated and reconsidered following review of the literature. The necessity for right reflux brachial angiography is emphasized for early diagnosis of extradural hemorrhage.

Birth Injuries↗