Purification and partial characterization of acyl carrier protein from Euglena gracilis variety bacillaris.
Acyl carrier protein (ACP) was purified from Euglena gracilis variety bacillaris in yields of about 1 mg/100 g (wet wt) of cells. Antibodies against the purified protein were raised in hens and isolated from eggs. Antibodies raised against Euglena ACP inhibited the Euglena chloroplast nonaggregated fatty acid synthetase using either Euglena or Escherichia coli ACP as a substrate. Comparisons with other ACPs included the following items: biologic activity, acidic pI, size, behavior in size exclusion media, and amino acid sequence of the N-terminal portion of the molecule.
Williams
S G
SG
Department of Biochemistry, James H. Quillen College of Medicine, East Tennessee State University, Johnson City 37614.
Worsham
L M
LM
Ernst-Fonberg
M L
ML
D000213:Acyl Carrier Protein / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000818:Animals; D004926:Escherichia coli / Q000737:chemistry; D005056:Euglena gracilis / Q000737:chemistry*; D007120:Immunochemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D000213:Acyl Carrier Protein