Extracellular production of human growth hormone by a head portion of the prepropeptide derived from Bacillus amyloliquefaciens neutral protease in Bacillus subtilis

Nakayama, Akira; Kawamura, K.; Shimada, Hiroaki; Akaoka, Akiko; Mita, I.; Honjo, Masaru; Furutani, Yoshio

doi:10.1016/0168-1656(87)90014-9

Cited by 14 publications

(2 citation statements)

References 9 publications

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“…Salting-out processes, with ammonium sulfate in particular, have been in wide use since that time; Englard and Seifter (1990) have estimated that up to 80% of published protein purification protocols involve at least one salting-out step. The use of precipitation ranges from primary isolation procedures (Nakayama et al, 1987;Michaels, 1990) for the separation of product protein from cell debris in recombinant cell cultures, to finishing operations (Bell et al, 1983;Paul and Rosas. 1990) for the production of solids prior to drying and formulation.…”

mentioning

confidence: 99%

Protein precipitation: Effects of mixing on protein solubility

Iyer

Przybycien

1994

AIChE Journal

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mentioning

confidence: 99%

Protein precipitation: Effects of mixing on protein solubility

Iyer

Przybycien

1994

AIChE Journal

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“…The efficiency of chromatographic separations is largely dependent on upstream precipitation procedures (Englard & Seifer, 1990). Up to 80% of published protein purification protocols include at least one precipitation step, ranging from primary isolation [separating cellular debris from protein product in recombinant cell cultures (McGregor, 1983;Nakayama et al, 1987)] to finishing operations [producing solids prior to drying and formulation (Hoare et al, 1983;Paul & Rosas, 1990)], to yield a partially purified product of reduced volume (Chen et al, 1992;Englard & Seifer, 1990). Precipitation processes also rapidly isolate protein products, reducing their exposure to denaturing conditions and proteolytic enzymes (Chen et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Protein purification with vapor-phase carbon dioxide

Winters

Frankel

Debenedetti

et al. 1999

Biotechnol. Bioeng.

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Gaseous CO2 was used as an antisolvent to induce the fractional precipitation of alkaline phosphatase, insulin, lysozyme, ribonuclease, trypsin, and their mixtures from dimethylsulfoxide (DMSO). Compressed CO2 was added continuously and isothermally to stationary DMSO solutions (gaseous antisolvent, GAS). Dissolution of CO2 was accompanied by a pronounced, pressure‐dependent volumetric expansion of DMSO and a consequent reduction in solvent strength of DMSO towards dissolved proteins. View cell experiments were conducted to determine the pressures at which various proteins precipitate from DMSO. The solubility of each protein in CO2‐expanded DMSO was different, illustrating the potential to separate and purify proteins using gaseous antisolvents. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS‐PAGE) was used to quantify the separation of lysozyme from ribonuclease, alkaline phosphatase from insulin, and trypsin from catalase. Lysozyme biological activity assays were also performed to determine the composition of precipitates from DMSO initially containing lysozyme and ribonuclease. SDS‐PAGE characterizations suggest that the composition and purity of solid‐phase precipitated from a solution containing multiple proteins may be accurately controlled through the antisolvent's pressure. Insulin, lysozyme, ribonuclease, and trypsin precipitates recovered substantial amounts of biological activity upon redissolution in aqueous media. Alkaline phosphatase, however, was irreversibly denaturated. Vapor‐phase antisolvents, which are easily separated and recovered from proteins and liquid solvents upon depressurization, appear to be a reliable and effective means of selectively precipitating proteins. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 62: 247–258, 1999.

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Secretory expression of human growth hormone inSaccharomyces cerevisiae using three different leader sequences

Hahm

Chung

2001

Biotechnol. Bioprocess Eng.

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Extracellular production of human growth hormone by a head portion of the prepropeptide derived from Bacillus amyloliquefaciens neutral protease in Bacillus subtilis

Cited by 14 publications

References 9 publications

Protein precipitation: Effects of mixing on protein solubility

Protein precipitation: Effects of mixing on protein solubility

Protein purification with vapor-phase carbon dioxide

Secretory expression of human growth hormone inSaccharomyces cerevisiae using three different leader sequences

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