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Biomedical subjects

K Matsuda

Publications and source records attributed to K Matsuda.

At least 775 records · Page 43Linked to original sources
PubMed1981

Representation of the masticatory muscles in the motor trigeminal nucleus of the macaque monkey.

The pattern of representation of the masticatory muscles in the motor trigeminal nucleus was examined in macaque monkeys by the horseradish peroxidase method. The motor trigeminal nucleus was divided cytoarchitectonically into the dorsolateral and ventromedial divisions. The temporalis, masseter and pterygoid muscles were represented in the dorsomedial, central and ventrolateral parts of the dorsolateral division, respectively. In the ventromedial division, which was located at the level of the caudal half of the nucleus. The anterior digastric or mylohyoid muscle was represented in the dorsomedial or ventrolateral part of the division, respectively.

Animals↗
PubMed1981

Action of pancreatic juice on the bile duct: pathogenesis of congenital choledochal cyst.

Babitt was the first to suggest that the anomalous arrangement of the pancreatico-biliary ducts might be involved in the etiology of congenital choledochal cyst. Since then, many authors have reported this condition frequently associated with congenital choledochal cyst. The reflux of pancreatic juice into the common bile duct due to this anomaly has been thought to be responsible for the formation of choledochal cyst. Our previous study using the animal model with anomalous arrangement of pancreaticobiliary ducts, has proven that pancreatic juice in the common bile duct caused cystic dilatation of the common bile duct. However, the mode of action of pancreatic juice on the biliary duct has remained unclear. The present study using peroxidase as a tracer for permeability of the biliary duct showed early damage of the intercellular junction of biliary epithelium exposed by pancreatic juice, followed by affection of submucosal tissue.

Animals↗
PubMed1981

Biosynthesis of xyloglucan in suspension-cultured soybean cells. An assay method for xyloglucan xylosyltransferase and attempted synthesis of xyloglucan from UDP-D-xylose.

Hydrolysis of the total non-cellulosic 14C-polysaccharides from soybean cell wall with carbohydrate hydrolases of an Aspergillus oryzae enzyme preparation yielded 14C-monosaccharides and [14C]isoprimeverose (6-O-alpha-D-xylopyranosyl-D-glucopyranose) in which all of the xylosyl residues of the xyloglucan were recovered. Based on this finding, an assay method for the activity of xyloglucan xylosyltransferase was developed. When UDP-[14C]xylose was incubated with a particulate enzyme fraction from soybean cells, radioactive polymers were synthesized. On digestion with the A. oryzae enzyme preparation, the product gave 14C-monosaccharides and [14C]isoprimeverose. This result suggests that the activity of xyloglucan xylosyltransferase can be distinguished from other polysaccharide synthase activities.

Aspergillus oryzae↗
PubMed1981

Structure of the alkali-insoluble skeletal glucan of Lentinus edodes.

An alkali-insoluble core material was isolated from the fruit bodies of Lentinus edodes after exhaustive extraction with 24% NaOH at 5 degrees C. This material consists mainly of glucan which is closely associated with chitin. Methylation analysis has shown that the glucan part of the core material (skeletal glucan) has a highly branched structure with 1,6 and 1,3 linkages in a molar ratio of 2 : 1. Stepwise enzymatic hydrolysis with basidiomycete sp. QM 806 beta-1,3-glucanase has indicated the heterogeneity of the skeletal glucan. The outer part of the skeletal glucan seems to be composed mainly of beta-1,3 and beta-1,6 glucoside linkages and has a close structural similarity to lentinan, a water-soluble beta-glucan from L. edodes. The middle part of the skeletal glucan appears to be composed mainly of beta-1,6 glucoside linkages. The innermost part of the skeletal glucan is a highly branched glucan with beta-1,6 and beta-1,3 linkages. Probably, it is associated with chitin and a small amount of amino acid polymer.

Basidiomycota↗
PubMed1981

Stress-induced osmotic adjustment in growing regions of barley leaves.

Young barley seedlings were stressed using nutrient solutions containing NaCl or polyethylene glycol and measurements were made of leaf growth, water potential, osmotic potential and turgor values of both growing (basal) and nongrowing (blade) tissues. Rapid growth responses similar to those noted for corn (Plant Physiology 48: 631-636) were obtained using either NaCl or polyethylene glycol treatments by which exposure of seedlings to solutions with water potential values of -3 to -11 bars effected an immediate cessation of leaf elongation with growth resumption after several minutes or hours. Latent periods were increased and growth resumption rates were decreased as water potential values of nutrient solutions were lowered. In unstressed transpiring seedlings, water potential and osmotic potential values of leaf basal tissues were usually -6 to -8 bars, and -12 to -14 bars, respectively. These tissues began to adjust osmotically when exposed to any of the osmotic solutions, and hourly reductions of 1 to 2 bars in both water potential and osmotic potential values usually occurred for the first 2 to 4 hours, but reduction rates thereafter were lower. When seedlings were exposed to solutions with water potential values lower than those of the leaf basal tissues, growth resumed about the time water potential values of those tissues fell to that of the nutrient solution. After 1 to 3 days of seedling exposure to solutions with different water potential values, cumulative leaf elongation was reduced as the water potential values of the root medium were lowered. Reductions in water potential and osmotic potential values of tissues in leaf basal regions paralleled growth reductions, but turgor value was largely unaffected by stress. In contrast, water potential, osmotic potential, and turgor values of leaf blades were usually changed slightly regardless of the degree and duration of stress, and blade water potential values were always higher than water potential values of the basally located cells. It is hypothesized that blades have high water potential values and are generally unresponsive to stress because water in most of the mesophyll cells in this area does not exchange readily with water present in the transpiration stream.

Journal Article↗
PubMed1981

Comparison of the mannan structure from the cell-wall mutant Candida sp. M-7002 and its wild type. I. Characterization of the proteo-mannan from the mutant and the wild-type cells.

The cell-wall mutant of a hydrocarbon-assimilating yeast, Candida sp. M-7002 and its wild type have shown a significant difference in mannose content. Each mannan was isolated from the mutant and the wild-type cells by fractionation with Cetavlon and copper reagent. Both mannans contain D-mannose, D-glucose and phosphate. The mutant mannan has a relatively high content of protein (18% in weight bases) whereas the wild-type mannan has a low protein content (5.1%) with a high amount of carbohydrate (greater than 90%). Structural analyses by enzymatic and chemical methods showed that both mannans had a mannosidic (alpha 1--6)-linked back bone substituted at O-2 by side chains of varying length. The side chains of the mutant mannan were shown to consist of single mannose units and disaccharide units whose linkages were predominantly alpha 1--2, while the wild-type mannan had two additional side chains of disaccharides. These additional side chains had alpha 1--3 linkages which were scarcely found in the mutant mannan. beta-Elimination reaction demonstrated that the mannans also contain mannosyl oligosaccharides linked to protein through O-glycosidic linkage. The chemical properties of the mannan of the Candida mutant indicates that the mutation might occur not only in the side chain structure but also in the (alpha 1--6)-linked mannan back bone.

Candida↗
PubMed1981

Comparison of the mannan structure from the cell-wall mutant Candida sp. M-7002 and its wild type. II. Immunochemical properties of the mannans.

The structure of the proteomannans from the cell-wall mutant Candida sp. and its parent strain was further studied by immunochemical methods. Alkaline titration showed that the phosphate is present in the form of diester and mild acid treatment released mannose from both of the mannans. In the wild-type mannan, the phosphorylated side-chain oligosaccharides gave 85% inhibition and a mannopentaose side chain having alpha 1--3 linkage in the nonreducing terminal also gave 40% inhibition in the homologous precipitin reaction. This indicates that the immunodominant side chain of the Candida sp. wild type mannan is the phosphorylated mannopentaose which has an (alpha 1--3)-linked nonreducing terminal. In the mutant system, a significant reactivity in the cross reaction between the mutant antiserum and Kloeckera brevis mannan indicates that the immunodeterminant of the mutant mannan may be a structural analogue of the side-chain oligosaccharide from K. brevis, which has phosphorylated (alpha 1--3)-linked mannotriose. However, no definite results were obtained in the inhibition studies. On the basis of the results from chemical, enzymatical and immunological experiments, the side-chain structure and macromolecular models of Candida sp. wild-type and mutant mannans are proposed.

Antigen-Antibody Complex↗
PubMed1981

Specular microscopy of the human lens.

Some specular features of the normal and abnormal human lens are described and recorded in vivo by macrophotography. Anteriorly the lens exhibits three distinct specular zones: a coarse shagreen, an epithelial pattern, and a lens fibre pattern. The posterior specular zone is relatively featureless. Uncorrected values for epithelial cell diameter in the central zone of the normal lens gave a mean of 13.9 microns. Lens fibre diameter in the same zone was 13.7 microns. The 'relief images' of the adult lens are also described, including perinuclear changes which have been termed retrodot lens opacities.

Adolescent↗
PubMed1980

Dextran alpha-(1 yields 2)-debranching enzyme from Flavobacterium Sp. M-73. Properties and mode of action.

The general properties and specificity of a dextran alpha-(1 yields 2)-debranching enzyme from Flavobacterium have been examined in order to apply this enzyme to the structural analysis of highly branched dextrans. The optimum pH range and temperature were pH 5.5-6.5, and 45 degrees, respectively. The enzyme was stable up to 40 degrees on heating for 10 min, and over a pH range of 6.5-9.0 on incubation at 4 degrees for 24 h. The effects of various metal ions and chemical reagents have also been examined. The debranching enzyme has a strict specificity for the (1 yields 2)-alpha-D-glucosidic linkage at branch points of dextrans and related branched oligosaccharides, and produces D-glucose as the only reducing sugar. The degree of hydrolysis of the dextrans by this enzyme and the Km value (mg/mL) were as follows: B-1298 soluble, 25.2%, 0.21; B-1299 soluble, 31.5%, 0.27; and B-1397, 11.8%, 0.91. the debranching enzyme thus has a novel type of specificity as a dextranhydrolase. We have termed this enzyme as dextran alpha-(1 yields 2)-debranching enzyme, and its systematic name is also discussed.

Cations↗