Expression of human. alpha. -fetoprotein in yeast

Journal Article · Mon Jan 01 00:00:00 EST 1990 · Life Sciences; (USA)

DOI:https://doi.org/10.1016/0024-3205(90)90383-3· OSTI ID:6705168

Yamamoto, Ritsu; Sakamoto, Takashi; Nishi, Shinzo; Sakai, Masaharu; Morinaga, Tomonori; Tamaoki, Taiki ^[1]

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1. Hokkaido Univ. School of Medicine (Japan) Univ. of Calgary, Alberta (Canada)

Human {alpha}-fetoprotein (AFP) was expressed in Saccharomyces cerevisiae, with a plasmid containing the cDNA sequence for human AFP fused with the rat AFP signal peptide. The recombinant AFP was purified from the yeast lysate by DEAE-cellulose and immunoaffinity chromatography. The amino acid composition and the molecular weight of the recombinant AFP were similar to those of hepatoma AFP. N-terminal amino acids sequence analysis indicated that the signal peptide had been processed. The recombinant and hepatoma AFP reacted identically in Ouchterlony immunodiffusion and radioimmunoassay tests. These observations indicated that the yeast recombinant protein had the properties of native AFP.

• OSTI ID: 6705168
• Journal Information: Life Sciences; (USA), Vol. 46:23; ISSN 0024-3205
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
GENE RECOMBINATION PROTEINS
RADIOIMMUNOASSAY
AMINO ACID SEQUENCE
CHROMATOGRAPHY
GENE REGULATION
MAN
MOLECULAR WEIGHT
PEPTIDES
PLASMIDS
SACCHAROMYCES CEREVISIAE
ANIMALS
BIOASSAY
CELL CONSTITUENTS
DIAGNOSTIC TECHNIQUES
EUMYCOTA
FUNGI
IMMUNOASSAY
IMMUNOLOGY
ISOTOPE APPLICATIONS
MAMMALS
MICROORGANISMS
MOLECULAR STRUCTURE
NUCLEOPROTEINS
ORGANIC COMPOUNDS
PLANTS
PRIMATES
PROTEINS
RADIOASSAY
RADIOIMMUNODETECTION
RADIOIMMUNOLOGY
SACCHAROMYCES
SEPARATION PROCESSES
TRACER TECHNIQUES
VERTEBRATES
YEASTS
550201* - Biochemistry- Tracer Techniques