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Biomedical subjects

T Matsuda

Publications and source records attributed to T Matsuda.

At least 1,675 records · Page 93Linked to original sources

Relative hemodynamic effectiveness of whole blood and plasma expanders in burned patients.

In a series of nine fatally burned patients, hemodynamic and oxygen transport measurements were made before, during and after 56 administrations of 500 milliliters of whole blood or colloids and 1,000 milliliters of crystalloids. To enhance comparability, 38 of these studies were conducted at intervals on the same patient, the patient serving as his own control. The data indicate greater hemodynamic responses to colloids than to whole blood and greater responses to whole blood than to crystalloids when the latter was given at twice the volume as well as at four times the volume of the colloid. The data suggest that, in addition to replenishing salt and water, restoration of hemodynamic and oxygen transport variables may be accomplished by expansion of plasma volume with colloids and whole blood. Adequate nutrition is also needed for the increased metabolic needs of the burned patient. Without supplemental nutrition, high grade plasma proteins and tissue proteins may be expended as energy substrates; the lowering of plasma proteins tends to redistribute water from the plasma to the interstitial phase, which increases further the peripheral edema.

Blood Pressure↗

Thiamine diphosphatase in rat small intestine.

TDPase is located mostly in the proximal portion of the small intestine and its activity, like that of ALPase, decreased markedly in thiamine deficiency. The decreased enzyme activities were restored after thiamine or vitamin D3. Kinetic and other studies of the purified enzyme indicated the identity of the two enzymes.

Alkaline Phosphatase↗

Studies on triglyceride lipases from rat adipose tissue.

A new assay procedure for triglyceride lipase [EC 3.1.1.3] was developed in which radioactive triolein was dissolved in ethanol and directly added to the reaction mixture in the absence of serum and albumin. In the rat adipose tissue there appeared to be a triglyceride lipase measurable with this assay in addition to the two previously defined lipases, lipoprotein lipase [EC 3.1.1.34] and hormone-sensitive lipase. The enzyme was active in the absence of serum and was strongly inhibited by albumin. The molecular weight was estimated to be about 42,000. Adenosine 3',5'-monophosphate-dependent protein kinase [EC 2.7.1.27] was unable to activate the enzyme. The three species of lipases mentioned above behaved differently upon chromatography on a Sepharose 4B column, and were distinguishable from each other in their physical and kinetic properties. The physiological roles of the new species of lipase remain to be explored.

Adipose Tissue↗

Effects of Na+ and other monovalent cations on Ca-efflux from synaptosomes.

Effects of monovalent cations on Ca-efflux were examined in rat brain cortex slices, synaptosomes and synaptic plasma membranes. Effluxes of 45Ca from brain slices and synaptosomes were stimulated by Na+ in medium and the effects of Na+ on the 45Ca-effluxes disappeared at low temperature. Furthermore, we observed that Rb+ had more effect than Na+ on 45Ca-efflux from the synaptosomes, while Li+ had less effect. On the other hand, release of 45Ca from the synaptic plasma membranes which had been preincubated with ATP, MG++ and 45Ca was stimulated by Na+ and Li+. But Cs+ and Rb+ were less effective on the release. These results indicate occurrence of Na-dependent Ca-efflux at nerve endings. However, the assumption that ATP-dependent Ca-binding with synaptic plasma membranes may be a partial reaction of Ca-efflux was not supported by these experiments.

Animals↗

Effects of La+++, Mn++ and ruthenium red on Mg-Ca-ATPase activity and ATP-dependent Ca-binding of the synaptic plasma membrane.

The effects of La+++, Mn++ and ruthenium red (R.R.) on Ca-uptake of synaptic plasma membranes (S.P.M.) were investigated. La+++ (0.1 mM), Mn++ (0.2 mM) and R.R. (0.1 mM) selectively inhibited Mg-Ca-ATPase but did not significantly affect Mg-ATPase activity. The apparent Ki values of La+++, Mn++ and R.R. for Mg-Ca-ATPase were 0.05, 0.06 and 0.03 mM, respectively. La+++, Mn++ and R.R. did not affect Ca-uptake at concentrations which strongly inhibited Mg-Ca-ATPase activity. These results indicate that Ca-uptake by S.P.M. differ from that by sarcoplasmic reticulum.

Adenosine Triphosphatases↗

Experimental pulmonary emphysema in Syrian hamsters.

Syrian hamsters were exposed to the aerosol of a 5% solution of papain in the presence of cysteine and ethylenediamine-tetraacetic acid. Pulmonary emphysema in hamsters was observed after exposure to papain for two to three hours. There was no change with time in the severity of emphysema from the second through the fourth weeks after exposure to papain. Pathogenesis of pulmonary emphysema was discussed in relation to proteolysis of glycosaminoglycan-protein complex.

Animals↗

Isolation and purification of D-alanyl-meso-2, 6-diaminopimelic acid endopeptidase of Streptomyces L-3 enzyme using soluble substrates of known chemical structure from Lactobacillus plantarum cell wall digests.

D-alanyl-meso-2, 6-diaminopimelic acid (D-Alanyl-meso-A2pm) endopeptidase was isolated and purified from a crude Streptomyces L-3 enzyme preparation by ion exchange chromatography and isoelectric focusing in a density gradient. During its purification, its hydrolytic activity was assayed on cell walls of Lactobacillus plantarum ATCC 8014 and soluble glycopeptides and peptides, of known chemical structures, prepared enzymatically from these cell walls. A fraction with an isoelectric point of pH 7.9 cleaved the bond between the carboxyl group of the D-alanine residue at the C-terminal in one peptide subunit and one of the two amino groups of the A2pm residue in the neighboring peptide subunit. Unlike the crude enzyme, the endopeptidase in this fraction showed no N-acetylmuramyl-L-alanine amidase, A2pm carboxyamide amidase or proteinase(s) activity and it was immunologically homogeneous.

Alanine↗