Method for recombinant yeast expression and isolation of water-soluble collagen-type polypeptides
US5710252A · kind A · utility
10Cited by
8References
22Claims
0Family size
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Key dates
| Filing date | Feb 3, 1995 |
| Grant date | Jan 20, 1998 |
| Priority date | — |
| Expiry date | Feb 3, 2015 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC07K14/78
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
A method for preparing and purifying collagen-type polypeptides (or biopolymers) has been developed. The polypeptides are prepared by recombinant DNA technology using yeast host cells. Once expressed in the host cell culture, the polypeptide is purified by a series of centrifugations, isoprecipitation, ion exchange (or other chromatography), and diafiltration steps. Treatments with a protease and a calcium salt are also carried out at some point. It is also desirable to diafilter the purified fractions from the last chromatography to exchange ions which make the resulting polypeptide more compatible with its intended use.
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.