Abstract
Botryllus schlosseri is a colonial marine invertebrate that belongs to the subphyllum Urochordata. Previously we analyzed the activity of a serine protease in this species, and cloned a tunicate chymotrypsin-like molecule. In the present study we further analyzed the protease activity of this animal, and found biochemical evidence also for specific trypsin-like activity. Subsequently we utilized a degenerate polymerase chain reaction (PCR) primer to clone two B. schlosseri cDNAs coding for two different putative trypsinogens, each 243 amino acids long, that differ within the coding region in 42 amino acids and 99 nucleotides. Both clones feature the characteristics of animal anionic trypsinogens. Sequence analysis of the tunicate putative trypsinogens revealed the invertebrate characteristics of three disulfide bridges, and higher similarity to invertebrate than to vertebrate trypsinogens. We therefore propose that the typical characteristics of vertebrate trypsinogens evolved after the divergence of Urochordates and Cephalochordates.
| Original language | English |
|---|---|
| Pages (from-to) | 326-333 |
| Number of pages | 8 |
| Journal | Molecular Marine Biology and Biotechnology |
| Volume | 5 |
| Issue number | 4 |
| State | Published - Dec 1996 |
| Externally published | Yes |
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology