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.
Département de Physiologie des Invertébrés, URA CNRS 1138, Université de Bordeaux 1, Talence, France.
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Lassalle
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Lassègues
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Roch
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