Kazuya Takeshima

TL;DR: In this article, the authors used a combination of specified steps in which a culture supernatant obtained from a human serum albumin-producing host is subjected to ultra-filtration, heat treatment, acid treatment and another ultrafiltration followed by subsequent treatments with a cation exchanger, a hydrophobic chromatography carrier and an anion exchanger.

TL;DR: The physicochemical and immunochemical properties of recombinant human serum albumin from Pichia pastoris with those of plasma-derived human serumalbumin (pHSA) are compared and the total amount of fatty acid was higher for pHSA than for rHSA.

TL;DR: The structure of recombinant human serum albumin derived from Pichia pastoris (rHSA) was analyzed in detail and agreed with the primary structure deduced from its cDNA.

TL;DR: A method for suppressing coloring of human serum albumin expressed by genetic engineering which comprises culture and/or purification in the presence of an amine compound selected from the group consisting of alkylamines, diamines, guanidines, benzamidine, basic amino acids, and aminophenylacetic acids is presented in this paper.

TL;DR: In this paper, the authors obtained an almost colorless human serum albumin free from contaminant components by purifying cultured supernatant of a human albumin- producing host by ultrafiltration, heating, acid treatment, cation and anion exchange treatment, hydrophobic chromatography, etc.