Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus).

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Laycock MV,MacKay RM,Di Fruscio M,Gallant JW

doi

10.1016/0014-5793(91)80847-v

subject

Has Abstract

pub_date

1991-11-04 00:00:00

pages

115-20

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80847-V

journal_volume

292

pub_type

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