ISSN:
1432-1793
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The fate of the protease trypsin in intestines of individual herring larvae Clupea harengus L. was studied following digestion of the copepod Acartia tonsa. Trypsin was retained in the intestine during two consecutive pulses of feeding and defaecation of copepods. Quantification of herring trypsin in digested, defaecated copepods showed that ca. 1% of larval intestinal enzyme was defaecated along with 1 to 3 copepods. Following ingestion of a single meal, the level of intestinal trypsin post-ingestion declined to pre-ingestion levels within 1 to 2 d of starvation. All enzyme data thus indicated that trypsin, released in response to ingestion of a meal, was retained. In addition, analysis of fed subgroups of starved larvae clearly indicated that release of trypsin from the pancreas stopped after 6 to 8 d of starvation. As the fish still contained substantial amounts of trypsinogen, the underlying cause might be defective release mechanisms. Daily secretion of trypsin and processes responsible for enzyme retention in the gut are discussed. Assimilation efficiency in herring larvae was estimated for copepodite prey. Average carbon assimilation was 90%.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00391042
