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Biomedical subjects

K Matsuda

Publications and source records attributed to K Matsuda.

At least 829 records · Page 46Linked to original sources
PubMed1978

Surgical and pathologic aspects of protein losing gastropathy.

The mechanism of protein loss from the gastric wall was investigated in patients with Ménétrier's disease, gastric polyps, and carcinoma of the stomach. In Ménétrier's disease, plasma protein was lost as glycoprotein in the gastric juice secreted from proliferated foveolar cells. Some of the gastric polyps also showed pathologic findings similar to that of Ménétrier's disease. As a treatment for the diffuse type of Ménétrier's disease, subtotal gastrectomy was recommended by presenting enough recovery from hypoproteinemia. A small amount of protein lost from the remaining portion of the stomach may be almost completely digested and reabsorbed from the intestine. In instances of carcinoma of the stomach, the mechanism of protein loss was speculated to be loss of lymph, blood or other interstitial fluids from opened capillaries of the cancerous surface. Complete removal of the carcinoma, therefore, certainly results in recovery from hypoproteinemia.

Blood Proteins↗
PubMed1977

Biosynthesis of glycogen in Neurospora crassa. Existence of a glucoproteic intermediate in the initiation process.

A soluble enzyme preparation (20,000 X g supernatant fraction), prepared from the mycelia of wild-type Neurospora crassa, was capable of transferring [14C]glucose from UDP-[14C]glucose into both trichloroacetic acid (TCA)-soluble and TCA-insoluble macromolecule products in the absence of added primer. These reactions did not require either high concentrations of salts or any other chemical reagents. Two labeled products were formed; one was a glycogen-like polysaccharide and the other was a glycoprotein with glucosyl chains bound to protein through an acid-labile bond. After mild treatment of the glucoprotein with acid, the product liberated from the protein behaved as a mixture of malto-oligosaccharides and alpha-1,4-glucan with branches. The carbohydrate moiety of the glucoprotein seemed to be released upon prolonged incubation with the enzyme preparation. The glucan thus liberated from the glucoprotein may serve as a primer for the glycogen synthase. The results obtained are therefore suggestive of the existence of a glucoproteic intermediate in the initiation of glycogen biosynthesis.

Carbohydrates↗
PubMed1977

A cell wall proteo-heteroglycan from Piricularia oryzae: isolation and partial structure.

A purified proteo-heterolgycan, [alpha]D + 72.5 degrees, was isolated from Piricularia oryzae, a pathogenic fungus of rice blast disease (Imochi-byo), by means of hot citrate buffer extraction, cetavlon fractionation, and DEAE-Sephade chromatography. It was found to be homogeneous by electrophoresis and by analytical ultracentrifugation to have an s value 6.1 and to contain 91% (w/w) of carbohydrate, which consists of D-mannose, D-glucose, and D-galactose in a molar ratio of 6:2:1. Partial acid hydrolysis and methylation analysis of the carbohydrate moiety of the proteo-heteroglycan indicate that the molecule is composed of mannan, the side chain terminals of which are partially modified with D-glucopyranose and D-galactofuranose. Enzymatic hydrolysis with bacterial alpha-D-mannanase has been shown to remove most of the side chains from the heteroglycan, leaving an (1-6) linked mannan back-bone with a small amount of side chains, the terminals of which must be modified with D-glucopyranose or D-galactofuranose. The carbohydrate to protein linkage of the proteo-heteroglycan was shown by alkaline beta-elimination, to be mannosyl serine or mannosyl threonine.

Amino Acids↗
PubMed1977

A cell wall proteo-heteroglycan from Piricularia oryzae: further studies of the structure.

The carbohydrate part of a proteo-heteroglycan from Piricularia oryzae was further studied by chemical and immunological methods. Acetolysis studies of the proteo-heteroglycan and exo-alpha-D-mannanase resistant core showed a (1 leads to 6) mannan back-bone structure with side chains composed of one to four mannose units, and some of which are terminated by D-glucose or D-galactofuranose. The mode of attachment of the terminal glucose was characterized to be alphaGlc(1 leads to 6)Man by inhibition reaction with oligosaccharides. Rabbit anti-serum formed against P. oryzae cells had three specificities, the first one for alphaGlc(1 leads to 6)alphamannosyl, the second one for alphaMan(1 leads to 3)alphamannosyl, and the last one for alphaGal-f(1 leads to 2)alphamannosyl residues. The most immunodominant side chain structure of the P. oryzae heteroglycan was shown to be alphaGlc(1 leads to 6)alphaMan(1 leads to 2)alphaMan(1 leads to 2)Man.

Carbohydrates↗