Yuko Yanagisawa

Analysis of the affinity of each haptoglobin polymer for hemoglobin by two-dimensional affinity electrophoresis.

Using polyacrylamide gel electrophoresis we have often encountered a decrease in the high molecular weight polymers of haptoglobin 2-1 in the serum of patients after transfusion and with hemolytic diseases. Using two-dimensional affinity electrophoresis we have attributed this phenomenon to the high affinity of high molecular weight polymers of the haptoglobin 2-1 for hemoglobin.

Synthesis of 2-amino-2-deoxy-D-hexopyranosides from 4-O-trichloroacetimidyl-D-hex-2-enopyranoside by [3,3]-sigmatropic rearrangement

2-Amino-2-deoxysugars, D-mannosamine and D-altrosamine derivatives were synthesized together with D-idosamine and D-talosamine ones from a 2-deoxy-2-trichloroacetamido-hex-3-enopyranoside. This key intermediate was prepared by regio- and stereoselective [3,3]-sigmatropic rearrangement of 4-O-trichloroacetimidyl-hex-2-enopyranoside.

Association equilibrium of d-methamphetamine and l-methamphetamine with serum albumin

The association equilibria for complex formation between serum albumin (bovine, rat) and the optical isomers of methamphetamine (MAMP) was determined using an ultrafiltration method. It was found that serum albumin/d-MAMP and serum albumin/l-MAMP complexes had distinctly different Scatchard plots with bovine and rat albumin. The binding parameters of each association equilibrium were estimated from the Scatchard plots by Rosenthals graphic method. This distinguished two kinds of specific binding sites in terms of the association equilibrium between bovine serum albumin and d-MAMP, and one binding site for rat serum albumin and d-MAMP. One specific binding site was found between serum albumin and l-MAMP in both bovine and rat. Molar ellipticities, [theta], of peaks were decreased in the CD spectra of the complexes formed between bovine serum albumin and d-MAMP or l-MAMP when compared with the CD spectrum of bovine serum albumin alone. However, no difference in [theta] was found between the CD spectra of the enantiomers of MAMP in the measured wavelength range. The non-specific binding site was distinct from the specific binding site and resulting from altered tertiary structure of the albumin molecule.

Studies on the human monocyte antigen.

We studied a random sample of Japanese and compared both Japanese and German monocyte antigen frequencies and performed a segregation analysis in Japanese families. In Japanese, the following gene frequencies were established: 0.0801 for HMA-A1; 0.0219 for HMA-A3; 0.0096 for HMA-A6; 0.1796 for HMA-B2; 0.0024 for HMA-B4. The data of the gene frequency in German were presented by Rose (0.1340 for HMA-A1; 0.0315 for HMA-A3; 0.0096 for HMA-A6; 0.1796 for HMA-B2; 0.0024 for HMA-B4). In this comparison, the frequency for HMA-B4 in German is more than twelve times higher. For antigen HMA-A1, the Japanese is a half of the German quantity. The antigen HMA-A6 and HMA-B4 were very rare in Japanese. The results we obtained from family analysis confirmed an unambiguous autosomal, codominant inheritance of the examined HMA antigens.