Recombinant protein expression in Pichia pastoris

被引：932

作者：

Cregg, JM

Cereghino, JL

Shi, JY

Higgins, DR

机构：

[1] Keck Grad Inst Appl Life Sci, Claremont, CA 91711 USA

[2] Oregon Grad Inst Sci & Technol, Beaverton, OR 97006 USA

[3] Idun Pharmaceut, La Jolla, CA 92037 USA

来源：

MOLECULAR BIOTECHNOLOGY | 2000年 / 16卷 / 01期

关键词：

Pichia pastoris; Pichia methanolica; methylotrophic yeast; heterologous protein production; foreign gene expression; yeast protein expression; fermentation;

D O I：

10.1385/MB:16:1:23

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The methylotrophic yeast Pichia pastoris is now one of the standard tools used in molecular biology for the generation of recombinant protein. P. pastoris has demonstrated its most powerful success as a large-scale (fermentation) recombinant protein production tool. What began more than 20 years ago as a program to convert abundant methanol to a protein source for animal feed has been developed into what is today two production system. To date well over 200 heterologous proteins have been expressed in P. pastoris. Significant advances in the development of new strains and vectors, improved techniques, and the commercial availability of these tools coupled with a better understanding of the biology of Pichia species have led to this microbe's value and power in commercial and research labs alike.

引用

页码：23 / 52

页数：30

共 310 条

[11] A glycosyl hydrolase activity of mammalian reovirus σ1 protein can contribute to viral infection through a mucus layer
Bisaillon, M
Sénéchal, S
Bernier, L
Lemay, G
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1999, 286 (03) : 759 - 773
[12] Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda 1 protein
Bisaillon, M
Bergeron, J
Lemay, G
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (29) : 18298 - 18303
[13] Zinc-binding of endostatin is essential for its antiangiogenic activity
Boehm, T
O'Reilly, MS
Keough, K
Shiloach, J
Shapiro, R
Folkman, J
[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1998, 252 (01) : 190 - 194
[14] Boehm T, 1999, YEAST, V15, P563, DOI 10.1002/(SICI)1097-0061(199905)15:7<563::AID-YEA398>3.0.CO
[15] 2-R
[16] A group of α-1,4-glucan lyases and their genes from the red alga Gracilariopsis lemaneiformis:: purification, cloning, and heterologous expression
Bojsen, K
Yu, SK
Kragh, KM
Marcussen, J
[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1999, 1430 (02): : 396 - 402
[17] A new tool for studying the molecular architecture of the fungal cell wall:: one-step purification of recombinant Trichoderma β-(l-6)-glucanase expressed in Pichia pastoris
Bom, IJ
Dielbandhoesing, SK
Harvey, KN
Oomes, SJCM
Klis, FM
Brul, S
[J]. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1998, 1425 (02): : 419 - 424
[18] Efficient expression of the gene for spinach phosphoribulokinase in Pichia pastoris and utilization of the recombinant enzyme to explore the role of regulatory cysteinyl residues by site-directed mutagenesis
Brandes, HK
Hartman, FC
Lu, TYS
Larimer, FW
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (11) : 6490 - 6496
[19] Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotropic yeast Pichia pastoris
Brankamp, RG
Sreekrishna, K
Smith, PL
Blankenship, DT
Cardin, AD
[J]. PROTEIN EXPRESSION AND PURIFICATION, 1995, 6 (06) : 813 - 820
[20] Cloning of the patatin-like latex allergen Hev b 7, its expression in the yeast Pichia pastoris and its immunological characterization
Breiteneder, H
Sowka, S
Wagner, S
Krebitz, M
Hafner, C
Kinaciyan, T
Yeang, HY
Scheiner, O
[J]. INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY, 1999, 118 (2-4) : 309 - 310

← 1 2 3 4 5 6 7 8 9 10 →