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Biomedical subjects

K Yamato

Publications and source records attributed to K Yamato.

At least 91 records · Page 5Linked to original sources
PubMed1983

[Intrathoracic administration of adriamycin with closed tube thoracostomy drainage for malignant pleuritis: observation on the administration dosage].

The effect of intrathoracic administration of adriamycin with closed tube thoracostomy drainage was investigated on patients with various malignant pleural effusions (13 lung cancer and one each stomach, breast, ovarian cancer, respectively). The doses of adriamycin ranged from 50, 30, 20, to 10 mg given to four groups of 4 cases respectively. Comparative study on effective rates, survival period after the administration, side effects and histopathological changes in autopsied cases was performed. The results obtained were as follows: 1. With regard to effective rates and histopathological changes, no difference was observed in the four groups in term of dose escalation of Adriamycin. 2. 50% survival period was similar within the groups administered 20, 30 and 50 mg of Adriamycin. However, the group receiving 10 mg showed slightly shorter survival period. 3. Although serious side effects were not observed in any groups, minor toxicities were mostly encountered in the 50 mg group. 4. It was concluded that in the treatment of malignant pleural effusion, an appropriate dose of intrathoracic administration of adriamycin was about 20-30 mg.

Adenocarcinoma↗
PubMed1982

Biosynthesis of lactosylceramide and paragloboside by human lactose synthase A protein.

Lactosylceramide and paragloboside were synthesized from their precursor glycolipids and UDP-galactose by lactose synthase A protein [UDP-Gal : GlcNAc beta-4-galactosyltransferase, EC 2.4.1.22] purified to homogeneity from human plasma. The partially purified human liver enzyme and an extract from human lymphoblastoid cells also exhibited the above activities. Rabbit antibody against the purified human plasma lactose synthase A protein neutralized the glycolipid synthesis activity as well as the activity for lactose synthesis by the enzyme preparations from plasma, liver and lymphoblastoid cells. These results suggest that lactose synthase A protein existing in plasma, liver and lymphoblastoid cells can synthesize not only lactose but also lactosylceramide and paragloboside in vitro. The enzyme could play a role in the synthesis of these two glycolipids in vivo.

Animals↗
PubMed1982

A case of weak blood group B expression (Bm) associated with abnormal blood group galactosyltransferase.

The mechanisms of unusually weak A and B blood group expressions have not been well understood. Since the human blood group A and B substances are produced by the action of blood group GalNAc transferase and Gal transferase, respectively, the mechanism may be elucidated by examining the properties of the blood group transferases and membranes of the subjects with the abnormality. We examined a case associated with very weak B activity in red blood cells, an absence of the B agglutinin in serum, and an existence of the H and B substances in saliva, i.e., a case commonly classified as Bm. More than 85% of H sites remained unglycosylated in the subject's red cell membranes. The blood group Gal transferase activity in the subject's plasma and red cell membranes was about 50% of that of normal. The pH-activity profile and the Michaelis constants for UDP-Gal and 2'-fucosyllactose of the subject's enzyme were distinctively different from that of normal enzyme. These findings led us to conclude that the weak B activity in the present Bm case was due to a direct mutation in B gene resulting in formation of variant B enzyme with low affinity to UDP-Gal and insufficient galactosylation of H sites in the subject.

ABO Blood-Group System↗
PubMed1981

Thirteen cases of pyruvate kinase deficiency found in Japan.

Thirteen cases of pyruvate kinase (PK) deficiency, considered to be heterozygous for different PK mutants because of no consanguinities in their parents, were characterized by the International Committee for Standardization in Haematology (ICSH) recommended methods. These deficiency cases are named PK "Kagoshima," PK "Kyoto," PK "Takamatsu," PK "Abeno," PK "Kobe," PK "Marugame," PK "Hoenzaka," PK "Osaka," PK "Motomachi," PK "Gifu," PK "Hiroshima" PK "Matsumoto," and PK "Tama." The characteristics of mutant PK enzymes suggest that the cause of chronic hemolysis depends mainly on decreased affinity for phosphoenolpyruvate, thermolability, increased inhibition by adenosine triphosphate, and low activation by fructose-1, 6-diphosphate.

Adolescent↗
PubMed1981

Red-cell enzyme activities and properties of mutant pyruvate kinase after 1-year storage in a -80 degrees C freezer.

Red cells from 5 healthy adults and an unstable mutant pyruvate kinase (PK), PK Maebashi, were stored for 12 months in a -80 degrees C freezer. With an exception of triosephosphate isomerase and phosphoglycerate kinase activities, normal red-cell enzyme activities remained essentially unchanged. Mutant PK was characterized by the methods recommended by the International Committee for Standardization in Haematology (ICSH). Normal control and PK Maebashi remained essentially unchanged in their characteristics after storage in a -80 degrees C freezer for 12 months. These results indicate that the red cells stored over a long term in a -80 degrees C freezer can be used for the study of unstable mutant PK.

Blood Preservation↗
PubMed1980

Seven pyruvate kinase variants characterized by the ICSH recommended methods.

Seven new red-cell pyruvate kinase (PK) variants were characterized by the methods recently recommended by the International Committee for Stanardization in Haematology. The cases were all true homozygote as evidenced by consanguineous marriages of the parents; all are Japanese. These variants were designated as PK Tokyo, PK Nagasaki, PK Sapporo, PK Maebashi, PK Itabashi, PK Fukushima and PK Aizu, respectively. Low substrate affinity (high K0.5S for phosphoenolpyruvate) and thermal instability appear to play major roles in causing defective enzyme function, resulting in chronic haemolytic anaemia. Product inhibition of PK by ATP may also play an additional role in causing haemolysis in more than half the cases.

Adolescent↗
PubMed1975

Blood group A activities of glycoprotein and glycolipid from human erythrocyte membranes.

It is known that ABO blood group substances in human erythrocyte membranes are sphingoglycolipids, but recently several authors have reported that the glycoproteins of the erythrocyte membranes also have ABO blood group activities in addition to MN blood group activities and virus hemagglutination inhibitor activity. We solubilized blood group A erythrocyte membranes with lithium diiodosalicylate and separated the glycoprotein fraction by phenol extraction and ethanol precipitation. This fraction was apparently not contaminated with glycolipid, but it showed weak blood group A activity. The activity of the glycoprotein of the erythrocyte membranes was one-sixth of that of the lgycolipid fraction from the same amount of membranes. The glycoprotein components were purified by Sephadex G-200 gel filtration in SDS. The main component isolated, PAS 1, still showed blood A activity.

ABO Blood-Group System↗