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A Hitoi

Publications and source records attributed to A Hitoi.

15 recordsLinked to original sources
PubMed1990

[Patho-physiological analysis on peripheral circulation using thermography as an example of functional body imaging].

The various body imaging systems can be classified into structural body imaging and functional body imaging. Thermography is a typical example of the latter category. Thermography is regarded to mainly represent peripheral circulatory function on hands and feet. We have studied the patho-physiology of peripheral circulation in normal subjects and in patients with diabetic microangiopathy, using the thermography system. Analysis of the cold loading test by thermography revealed that the recovery after cold loading was decreased with aging in healthy subjects. In diabetic patients, recovery after cold loading was apparently lower than in senile healthy subjects on foot. Thermography was also considered as a useful tool for evaluation of the effect of medicines such as PGE1, in a long-term study, as well as single dose test. Furthermore, thermography proved to be the first choice study in serious peripheral circulatory failure such as diabetic gangrene, since it is a non-invasive and non-contact examination.

Aged↗
PubMed1987

The carbohydrate moieties of human urinary ribonuclease UL.

Ribonuclease UL purified from pooled human urine contains approximately 20.7% of neutral sugar and 7.8% of aminosugar. All sugars were quantitatively released as oligosaccharides on hydrazinolysis. The oligosaccharides were converted to tritium-labeled oligosaccharides on reduction with NaB3H4. The radioactive oligosaccharide fraction was separated into a neutral and an acidic fraction on paper electrophoresis. All oligosaccharides in the acidic fraction could be converted to neutral oligosaccharides with the release of one sialic acid residue by sialidase digestion. Both fractions were shown to be mixtures of more than fourteen oligosaccharides by gel permeation chromatography. Structural studies on these oligosaccharides involving sequential exoglycosidase digestion in combination with methylation analysis revealed that ribonuclease UL contains sialylated and non-sialylated mono, bi-, tri-, and tetraantennary complex type sugar chains with N-acetyllactosamine outer chains, and tri- and tetraantennary complex type sugar chains with various numbers of Gal beta 1----4GlcNAc beta 1----3Gal beta 1----4GlcNAc beta 1----outer chains. An important finding was that all sialic acid residues in the acidic oligosaccharides only occur as the Sia alpha 2----6Gal beta 1----4GlcNAc beta 1----2Man alpha 1----3 group. Both fucosylated and non-fucosylated trimannosyl cores were found among the asparagine-linked sugar chains of ribonuclease UL.

Carbohydrates↗
PubMed1986

Structures of sugar chains of human kidney gamma-glutamyltranspeptidase.

gamma-Glutamyltranspeptidase purified from human kidneys contains 4-5 asparagine-linked sugar chains in each molecule. The sugar chains were released from the polypeptide portion of the enzyme by hydrazinolysis as oligosaccharides and separated by paper electrophoresis into one neutral and two acidic fractions. By sequential exoglycosidase digestion and methylation analysis, the neutral fraction, which comprised 69% of total oligosaccharides, was shown to be a mixture of bisected bi- and triantennary complex-type sugar chains with and without a fucose on the proximal N-acetylglucosamine residue and with Gal beta 1----4GlcNAc and/or Gal beta 1----4(Fuc alpha 1----3)GlcNAc groups in their outer chain moieties. The acidic oligosaccharide fractions were mixtures of mono- and disialyl derivatives of bisected triantennary complex-type oligosaccharides with Gal beta 1----4GlcNAc and/or Gal beta 1----4(Fuc alpha 1----3)GlcNAc group in their outer chain moieties. Some of the outer chains of the acidic oligosaccharides were considered to be sialylated X-antigenic structures.

Carbohydrates↗
PubMed1985

The structures of the carbohydrate moieties of mouse kidney gamma-glutamyltranspeptidase: occurrence of X-antigenic determinants and bisecting N-acetylglucosamine residues.

Paper electrophoresis and Bio-Gel P-4 column chromatography of the oligosaccharides released from mouse kidney gamma-glutamyltranspeptidase by hydrazinolysis gave fractionation patterns quite distinct from those of the bovine and rat kidney enzymes. Structural studies of the fractionated oligosaccharides by sequential exoglycosidase digestion in combination with methylation analysis showed that mouse kidney gamma-glutamyltranspeptidase contains a series of bisected complex-type asparagine-linked sugar chains with the following oligosaccharides as their outer chain moieties: GlcNAc beta 1----, Sia alpha 2----Gal beta 1----4GlcNAc beta 1----, Gal beta 1----4(Fuc alpha 1----3)GlcNAc beta 1----, and sialylated N-acetyllactosamine repeating sugar chains. Some of these sugar chains were found for the first time in glycoproteins.

Acetylglucosamine↗
PubMed1984

Sialic acid-containing sugar chains of hen ovalbumin and ovomucoid.

The acidic oligosaccharide fractions released from hen ovalbumin and ovomucoid by hydrazinolysis contain both sialyloligosaccharides and sulfated oligosaccharides. The sialyloligosaccharides were converted into neutral oligosaccharides by sialidase digestion, and separated from sulfated oligosaccharides by paper electrophoresis. Structural studies of these neutral oligosaccharides showed that the oligosaccharides of ovalbumin have different structural characteristics from those of ovomucoid, i.e., all sialyloligosaccharides from ovomucoid contain a pentasaccharide, alpha-D-Manp-(1----3)-[alpha-D-Manp-(1----6)]-beta-D-Manp -(1----4)-GlcpNAc- (1----4)-GlcpNAc, as a common core, and the smallest oligomannosyl core of the sugar chains from ovalbumin is alpha-D-Manp-(1----3)-alpha-D-Manp-(1----6)-[alpha-D-Manp -(1----3)]-beta-D- Manp-(1----4)-GlcpNAc-(1----4)-GlcpNAc. By methanolysis followed by N-acetylation, sialyl oligosaccharides, free from sulfated oligosaccharides, were recovered quantitatively from the acidic fractions of ovalbumin and ovomucoid. Methylation analysis of these sialyloligosaccharide mixtures, before and after sialidase digestion, showed that all sialic acid of both glycoproteins occurs as a alpha-Sia-(2----3)-D-Galp group.

Animals↗
PubMed1984

Application of a Phaseolus vulgaris erythroagglutinating lectin agarose column for the specific detection of human hepatoma gamma-glutamyl transpeptidase in serum.

By making use of the structural change of the sugar chains of liver gamma-glutamyl transpeptidase associated with malignant transformation, a new method has been developed to distinguish human serum gamma-glutamyl transpeptidase associated with primary hepatoma from that of non-hepatoma patients. In principle, the method consists of affinity chromatography of the desialylated serum enzyme on a Phaseolus vulgaris erythroagglutinating lectin agarose column.

Carcinoma, Hepatocellular↗
PubMed1983

Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides.

The behaviors of oligosaccharides obtained by hydrazinolysis of asparagine-linked sugar chains in an erythroagglutinating phytohemagglutinin lectin-agarose column were examined to define the structural determinants required for the interaction of asparagine-linked sugars with erythroagglutinating phytohemagglutinin. The minimal structural unit required for erythroagglutinating phytohemagglutinin binding was (formula; see text) in which R1 and R2 represent either hydrogen or sugars and R3 represents either GlcNAc leads to Asn or (Fuc alpha 1 leads to 6)GlcNAcOT.

Carbohydrate Conformation↗
PubMed1983

Structural studies of the carbohydrate moieties of rat kidney gamma-glutamyltranspeptidase. An extremely heterogeneous pattern enriched with nonreducing terminal N-acetylglucosamine residues.

The carbohydrate moieties of gamma-glutamyltranspeptidase purified from rat kidney were released as oligosaccharides by hydrazinolysis. Fractionation of the oligosaccharide mixture by paper electrophoresis and Bi-Gel P-4 column chromatography and structural study of each component by sequential exoglycosidase digestion in combination with methylation analysis and periodate oxidation have revealed that it is composed of 23 neutral oligosaccharides, monosialyl derivatives of 67 oligosaccharides, disialyl derivatives of 62 oligosaccharides, and trisialyl derivatives of 5 oligosaccharides. The neutral oligosaccharides are either high mannose type or biantennary complex type, and the acidic oligosaccharides are bi-, tri-, and tetranntennary complex type sugar chains. Most of the complex type sugar chains contain an N-acetylglucosamine residue at the C-4 position of the beta-mannosyl residue of their trimannosyl core. Another characteristic feature of these complex type sugar chains is that they are enriched with nonreducing terminal beta-N-acetylglucosamine residues.

Animals↗
PubMed1983

Organ-specific difference in the sugar chains of gamma-glutamyltranspeptidase.

Sugar chains of gamma-glutamyltranspeptidase purified from neonatal mouse liver and adult mouse kidney were quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis. A comparative study of the structures of the oligosaccharides has revealed that the GlcNAc beta 1 leads to 4Man beta 1 leads to group is found in the sugar chains of kidney enzyme but not in those of liver enzyme. This is considered as an organ-specific difference common to mammals because the same phenomenon was found in bovine and rat enzymes.

Acyltransferases↗
PubMed1983

Difference in the sugar chains of two subunits and of isozymic forms of rat kidney gamma-glutamyltranspeptidase.

A comparative study by gel-permeation chromatographic analysis of oligosaccharides released from the heavy and the light subunits of rat kidney gamma-glutamyltranspeptidase has revealed that high-mannose-type sugar chains are found only in the heavy subunit, and the nonsialylated and nonfucosylated biantennary complex-type sugar chains are included only in the light subunit. By the same analysis of the oligosaccharide fractions obtained from four isozymic forms of rat kidney gamma-glutamyltranspeptidase, it was found that all these enzymes contain 2 mol of neutral sugar chains but different numbers of acidic sugar chains. The total numbers of sialic acid residues showed a reciprocal relationship to the isoelectric point of each isozymic form, and an increase of 1 mol of sialic acid residue corresponds to a decrease of 0.5 in the value of the isoelectric point.

Animals↗
PubMed1983

Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from rat liver and rat AH-66 hepatoma cells.

A comparative study using hydrazinolysis has revealed that the oligosaccharide pattern of gamma-glutamyltranspeptidase purified from rat AH-66 hepatoma cells is very different from that of the enzyme from rat liver. Studies of oligosaccharides in each fraction have clarified the structural basis of the difference found in the sugar chains of the two enzymes. The sugar chains of the liver enzyme were all acidic, while 28% of those of the hepatoma enzyme were neutral, the latter being composed of high-man-nose-type and complex-type sugar chains. Three prominent structural differences were found in the acidic sugar chains of the two enzymes: (a) the sugar chains of the liver enzyme have complete outer chains, Gal beta 1 leads to 4GlcNAc beta 1 leads to, while many of those of the hepatoma enzyme have incomplete outer chains without galactose (Gal); (b) the Gal beta 1 leads to 4GlcNAc beta 1 leads to Gal beta 1 leads to 4GlcNAc beta 1 leads to group is found in the sugar chains of the liver enzyme but not in those of the hepatoma enzyme; (c) more than 40% of the sugar chains of the hepatoma enzyme contain bisect N-acetylglucosamine (GlcNAc) residue which is not found in those of the liver enzyme. Furthermore, the total number of asparagine-linked sugar chains in one molecule of hepatoma enzyme was about 4 times that found in one molecule of liver enzyme.

Acyltransferases↗
PubMed1983

Sugar chain of alpha-fetoprotein produced in human yolk sac tumor.

The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis. The oligosaccharides were separated into a neutral and two acidic oligosaccharides by paper electrophoresis. By sequential exoglycosidase digestion in combination with per-O-methylation study and periodate oxidation, their structures were determined to be: Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(GlcNAc beta 1 leads to 4) (Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAcOT, Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(GlcNAc beta 1 leads to 4) (Sia alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAcOT; and Sia alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(GlcNAc beta 1 leads to 4) (Sia alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3)Man beta 1 leads to 4 GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAcOT, in which Gal is galactose, GlcNac is N-acetylglucosamine, Man is mannose, Fuc is fucose, Sia is sialic acid, and Subscript OT is the NaB3H4-reduced oligosaccharide.

Carbohydrate Sequence↗