Abstract: A means of controlling sugar chain-modification and sugar chain structure in the production of a glycoprotein with the use of gene recombination techniques. A process for producing a glycoprotein by culturing a gene recombinant host in a medium characterized in that the relative sugar consumption speed is employed as an indication and changed to thereby modify the sugar chain structure attached to the protein.

Abstract: A means of controlling sugar chain-modification and sugar chain structure in the production of a glycoprotein with the use of gene recombination techniques. A process for producing a glycoprotein by culturing a gene recombinant host in a medium characterized in that the relative sugar consumption speed is employed as an indication and changed to thereby modify the sugar chain structure attached to the protein.

Abstract: A production method of a heterologous protein, comprising culturing a heterologous protein-producing host prepared by gene manipulation in a medium containing a fatty acid or a salt thereof, and a surfactant and harvesting the heterologous protein from the culture. The production amount of the heterologous protein produced by a heterologous protein-producing host can be increased. Moreover, since decomposition of the heterologous protein by an enzyme derived from the host can be inhibited, enabling large scale production of a heterologous protein.

Abstract: A method for producing a desired protein, which comprises growing, by a fed-batch culture, a host cell capable of expressing the desired protein, wherein the specific growth rate of the host cell is changed from the initial rate to a predetermined one by successively changing the rate of addition of a substrate which controls the growth of the host cell. According to the mode of change of the rate of substrate addition to the medium of the present invention, optimal patterns of specific growth rate .mu. and specific production rate .rho. can be realized to optimize the fed-batch culture system. As a consequence of the realization, it is made possible to perform a high density culture of the host cell by fed-batch culture, an the desired protein can be produced efficiently in a short time.

Abstract: A process for producing recombinant human serum albumin (HSA) which comprises culturing an HSA producing host prepared by gene manipulation techniques at a temperature of from 21.degree. to 29.degree. C. Culturing the HSA producing host under such a specified temperature condition makes it possible to increase productivity of HSA production, improve the growth yield of an HSA producing host, and reduce the degree of coloring in the HSA preparation.

Abstract: A recombinant human serum albumin (rHSA) pharmaceutical preparation is sterilized by subjecting a pharmaceutical preparation of rHSA obtained by gene manipulation techniques packed in a container in an administration unit to heat treatment at 50.degree. to 80.degree. C. for 30 minutes or more. By the disclosed method, rHSA having high safety can be provided since microorganisms contaminated in rHSA pharmaceutical preparations die as a result of the sterilization method of the present invention.

Abstract: A process for producing recombinant human serum albumin (HSA) which comprises culturing an HSA producing host prepared by gene manipulation techniques at a temperature of from 21.degree. to 29.degree. C. Culturing the HSA producing host under such a specified temperature condition makes it possible to increase productivity of HSA production, improve the growth yield of an HSA producing host, and reduce the degree of coloring in the HSA preparation.

Abstract: A process for producing recombinant human serum albumin is disclosed, which comprises culturing a human serum albumin-producing host, prepared by gene manipulation techniques in a medium that contains an amino acid, preferably at least one amino acid selected from the group consisting of alanine, aspartic acid, glutamic acid, histidine, serine, tryptophan, valine, isoleucine, phenylalanine, cysteine and arginine, more preferably histidine. The process can significantly increase the yield of human serum albumin over that produced by known processes.