Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus)
Autor: | Laycock Mv, Gallant Jw, Di Fruscio M, MacKay Rm |
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Jazyk: | angličtina |
Předmět: |
Molecular Sequence Data
Restriction Mapping Biophysics Sequence alignment Biology Molecular cloning Cysteine proteinase Biochemistry Amino acid sequence Structural Biology Sequence Homology Nucleic Acid Complementary DNA Genetics Animals Cloning Molecular Molecular Biology Peptide sequence Homarus Base Sequence cDNA library Nucleic acid sequence DNA Cell Biology American lobster biology.organism_classification Molecular biology Nephropidae Blotting Southern Cysteine Endopeptidases Lobster cDNA cloning Digestive System Sequence Alignment |
Zdroj: | FEBS Letters. (1-2):115-120 |
ISSN: | 0014-5793 |
DOI: | 10.1016/0014-5793(91)80847-V |
Popis: | Three clones were isolated from a lobster digestive gland cDNA library, using oligonucleotide probes based on the partial amino terminal sequence of a digestive cysteine proteinase. The cDNAs, LCP1, LCP2 and LCP3 encode preproenzymes of 322, 323 and 321 amino acid residues, and putative mature enzymes of 217, 216 and 215 residues, respectively. Calculated mature protein molecular masses are 23386 (LCP1), 23093 (LCP2) and 23255 (LCP3) Sequence alignments show that the lobster enzymes are more similar to L (55–62% identity) than H (42–44%) or B (22–24%) cathepsins. Southern analysis indicated as many as eleven genes related to the three cDNAs. |
Databáze: | OpenAIRE |
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