Serological evidence and amino acid sequence of ubiquitin-like protein isolated from coelomic fluid and cells of the earthworm Eisenia fetida andrei.
1. A small protein of M(r) 10 kDa has been isolated by reverse-phase chromatography of the basic proteins contained in the coelomic fluid and cell lysate of the earthworm Eisenia fetida andrei. 2. The protein crossreacted in dot-blot with an anti-bovine ubiquitin antiserum. 3. Its N-terminal primary structure was determined by automatic Edman degradation on 26 consecutive amino acids and showed 69% (based on the 26 amino acids) or 82% (based on the first 19 consecutive amino acids) identity with many ubiquitins and similar charge and hydrophobicity profiles and secondary structure conformation.
Lassalle
F
F
Département de Physiologie des Invertébrés, URA CNRS 1138, Université de Bordeaux 1, Talence, France.
Lassègues
M
M
Roch
P
P
D000595:Amino Acid Sequence; D000818:Animals; D001826:Body Fluids / Q000378:metabolism*; D003429:Cross Reactions; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009835:Oligochaeta / Q000737:chemistry* / Q000166:cytology; D017386:Sequence Homology, Amino Acid; D014452:Ubiquitins / Q000737:chemistry / Q000276:immunology* / Q000302:isolation & purification
D014452:Ubiquitins