[논문]Production of Active Carboxypeptidase Y of Saccharomyces cerevisiae Secreted from Methylotrophic Yeast Pichia pastoris

RO, HYEON-SU; LEE, MI-SUN; HAHM, MOON-SUN; BAE, HEE-SUNG; CHUNG, BONG HYUN

Production of Active Carboxypeptidase Y of Saccharomyces cerevisiae Secreted from Methylotrophic Yeast Pichia pastoris 원문보기

Journal of microbiology and biotechnology, v.15 no.1, 2005년, pp.202 - 205

RO, HYEON-SU , LEE, MI-SUN (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology) , HAHM, MOON-SUN (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology) , BAE, HEE-SUNG (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology) , CHUNG, BONG HYUN (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology)

Abstract ▼ AI-Helper

Our previous study showed that the overexpression of carboxypeptidase Y (CPY) of Saccharomyces cerevisiae in Escherichia coli resulted in the formation of insoluble inclusion bodies. To produce soluble CPY, we designed a novel Pichia pastoris expression system, in which the following were inserted into expression vectors: three different signal sequences derived from the mating factor a1 of S. cerevisiae, an inulinase of Kluyveromyces marxianus, and the endogenous signal sequence of CPY. The expression vector pHIL-D2-SSinul-proCPY was the most effective in the production of proCPY among the vectors examined. The purified active CPY was obtained from proCPY by treating with proteinase K, followed by QExcellose ion-exchange column chromatography.

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참고문헌 (17)

Berne, P., S. Blanquet, and J. Schmitter. 1992. Carboxypeptidase Y-catalyzed transpeptidation of esterified oligo- and polypeptides and its use for the specific carboxyl-terminal labeling of proteins. J. Am. Chem. Soc. 114: 2603- 2610

상세보기
Blandin, G., L. Bertrand, A. Malpertuy, P. Wincker, F. Francois Artiguenave, and D. Dujon. 2000. Genomic exploration of the hemiascomycetous yeasts: 13 Pichia angusta. FEBS Lett. 48: 76-81

상세보기
Breddam, K., F. Widmer, and M. Meldal. 1991. Amidation of growth hormone releasing factor (1- 29) by serine carboxypeptidase catalysed transpeptidation. Int. J. Peptide Protein Res. 37: 153-160

상세보기
Buckler, D. R., E. Haas, and H. A. Scheraga. 1993. C-Terminal labeling of ribonuclease A with an extrinsic fluorescent probe by carboxypeptidase Y -catalyzed transpeptidation in the presence of urea. Anal. Biochem. 209: 20- 31

상세보기
Hahm, M. S., J. H. Bae, E. S. Choi, and B. H. Chung. 1999. In vitro activation of yeast pro-carboxypeptidase Y expressed as inclusion bodies in Escherichia coli. Biotechnol. Lett. 21: 881-885

상세보기
Hahm, M. S. and B. H. Chung. 2001. Refolding and purification of yeast carboxypeptidase Y expressed as inclusion bodies in Escherichia coli. Protein Express. Purif. 22: 101-107

상세보기
Hahm, M. S. and B. H. Chung. 2001. In vitro formation of active carboxypeptidase Y from pro-carboxypeptidase Y inclusion bodies by fed-batch operation. J. Microbiol. Biotechnol. 11: 887- 889

원문보기 상세보기
Henriksen, D. B., M. Rolland, M. H. Jakobsen, O. Buchardt, and K. Breddam. 1992. C-Terminal amidation of calcitonin by carboxypeptidase Y catalyzed transpeptidation with a photocleavable nucleophile. Peptide Res. 5: 321- 324
Henriksen, D. B., K. Breddam, and O. Buchardt. 1993. Peptide amidation by enzymatic transacylation and photolysis. Int. J. Peptide Protein Res. 41: 169- 180

상세보기
Ichikawa, K., Y. Shiba, Y. Jigami, and N. Serizawa. 1993. Secretion and overproduction of carboxypeptidase Y by a Saccharomyces cerevisiae ssll mutant strain. Biosci. Biotechnol. Biochem. 57: 1686-1690

상세보기
Kang, H. A., S. W. Nam, K. S. Kwon, B. H. Chung, and M. H. Yu. 1996. High-level secretion of human alpha 1antitrypsin from Saccharomyces cerevisiae using inulinase signal peptide sequence. J. Biotechnol. 48: 15- 24

상세보기
Kim, H. K., Y. K. Hong, H. E. Park, S. H. Hong, and Y. A. Joe. 2003. Secretory production of recombinant urokinase kringle domain in Pichia pastoris. J. Microbiol. Biotechnol. 13: 591- 597

원문보기 상세보기
Nielsen, T. L., S. Holmberg, and J. G. L. Petersen. 1990. Regulated overproduction and secretion of yeast carboxypeptidase Y. Appl. Microbiol. Biotechnol. 33: 307-312

상세보기
Ohi, H., W. Ohtani, N. Okazaki, N. Furuhata, and T. Ohmura. 1996. Cloning and characterization of the Pichia pastoris PRCl gene encoding carboxypeptidase Y. Yeast 12: 31- 40

상세보기
Shiba, Y., F. Fukui, K. Ichikawa, N. Serizawa, and H. Yoshikawa. 1998. Process development for high-level secretory production of carboxypeptidase Y by Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 50: 34- 41

상세보기
Winther, J. R. and P. Sorensen. 1991. Propeptide of carboxypeptidase Y provides a chaeperone-like function as well as inhibition of the enzymatic activity. Proc. Natl. Acad. Sci. USA 88: 9330- 9334

상세보기
Zhao, Y., W. Ge, Y. Gong, and C. Zhang. 2003. Cloning, expression, and renaturation studies of reteplase. J. Microbiol. Biotechnol. 13: 989- 992

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저자의 다른 논문 :

표제어: PCR

동의어: Packet Collision Rate

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