Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus).
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), 29093 (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.
Laycock
M V
MV
Institute for Marine Biosciences, National Research Council of Canada, Halifax, Nova Scotia.
MacKay
R M
RM
Di Fruscio
M
M
Gallant
J W
JW
D000818:Animals; D001483:Base Sequence; D015139:Blotting, Southern; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000235:genetics*; D004247:DNA / Q000235:genetics*; D004064:Digestive System / Q000201:enzymology*; D008969:Molecular Sequence Data; D008121:Nephropidae / Q000201:enzymology*; D015183:Restriction Mapping; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D004247:DNA; D003546:Cysteine Endopeptidases