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Y Isogai

Publications and source records attributed to Y Isogai.

At least 109 records · Page 6Linked to original sources

A new method of measuring red cell deformability and the effects of pentoxifylline.

The effect of pentoxifylline on red cell deformability was studied using a new device of a polycarbonate membrane filter ("Nuclepore') and a differential pressure type transducer. Differential pressure fluctuations due to the passage of red cells through the "Nuclepore' membrane were recorded as a differential pressure curve of red cell filtration. Red cell deformability was measured with a diluted red cell suspension (10 x 10(4)/mm3) in this buffered NaCl solution of normal osmotic pressure, 300m0sm/l as a suspending medium. Blood samples were taken from 9 healthy subjects and 26 patients with diabetes mellitus, liver disease and miscellaneous diseases. The ability of pentoxifylline to modify red cell deformability was investigated using concentrations of 20 micrograms/ml and 40 micrograms/ml in diluted red cell suspension which was incubated for 2 hours of 37 degrees C. Changes in red cell deformability were estimated from the gap between two differential pressure curves recorded in blood suspension with or without pentoxifylline. Addition of pentoxifylline increases red cell deformability in both groups of blood suspension in healthy subjects and patients. A significant increase in red cell deformability was observed in 40% of samples with the addition of 29 micrograms/ml pentoxifylline and in 77% of those with 40 micrograms/ml, respectively.

Adult↗

[Blood viscosity].

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Blood Viscosity↗

Enkephalin: conformational analysis by means of empirical energy calculations.

Low-energy conformations of methionine-enkephalin were generated by means of an empirical method of computation. Many compact conformations, including those containing various standard bends, were of comparable energy. However, one conformation was found to have a potential energy about 5 kcal/mol (21 X 10(3) J/mol) below that of the large group of compact conformations. In this conformation, the 3-glycyl and 4-phenylalanyl residues form a bend of type II'. The conformation is stabilized by a hydrogen bond between the OH group of the 1-tyrosine side chain and the C==O group of 3-glycine or 4-phenylalanine. The phenylalanine and methionine side chains are relatively unrestricted. The conformation is consistent with published nuclear magnetic resonance parameters--coupling constants, temperature dependence of the chemical shift, and spin-lattice relaxation times. It is likely that the molecule undergoes a conformational change when it is bound to the receptor. Leucine-enkephalin appears to have the same conformation as its methionine homolog.

Calorimetry↗

Tertiary structures of gastrin-like tetrapeptides.

Tertiary structures of gastrin-like tetrapeptide Trp-Met-Asp-Phe-NH2 and those substituted by Leu, Val or Gly for Met are studied. The lowest energy conformations of the side chains when the back bone is fixed in alpha-helix are obtained by modified minimization algorithm. It is suggested that protein folding proceeds in the accessible conformation space as a self-organization process leading to minimum energy conformation in this space.

Aspartic Acid↗