Digestive enzyme activities and their distribution in the alimentary canal of larvae of the three extant lamprey families.

Abstract:

:The activities of trypsin (EC 3.4.21.4), chymotrypsin (EC 3.4.21.1), lipase (EC 3.1.1.3) and amylase (EC 3.2.1.1) were measured in different regions of the alimentary tract of ammocoetes from each of the three extant lamprey families. In the southern hemisphere speciesGeotria australis (Geotriidae), and even more particularlyMordacia mordax (Mordaciidae), enzymatic activity was almost entirely confined to prominent diverticular extensions which arise at the oesophageal-intestinal junction. However, in the holarcticLampetra richardsoni (Petromyzontidae), which does not possess a diverticulum, the enzymatic activity was highest in the upper anterior intestine. It is not clear whether the presence of significantly higher amylolytic and lower lipolytic activities in the diverticulum ofG. australis than in the exocrine tissue of the other two species reflects interspecific differences in the composition of their diets. The capacity of exocrine tissue extracts for chymotryptic and tryptic digestion was assayed before and afterin vitro exposure to trypsin and enteropeptidase, their respective catalytic activators. Prior to exposure to these exogenous activators, both proteolytic enzymes were fully active inL. richardsoni, partially active inG. australis and totally inactive inM. mordax. Maximal chymotryptic activity was greater inM. mordax than inL. richardsoni andG. australis. In contrast, maximal tryptic activity was greater inL. richardsoni than inG. australis and was very low inM. mordax. Since trypsin is the only known activator of chymotrypsinogen, the negligible activity of trypsin inM. mordax would appear anomalous unless a trypsin inhibitor is present in the protopancreas of this species. Differences in the distribution of enzymatic activity within the alimentary tract of the three species is discussed in relation to proposed phylogenetic relationships amongst the extant lamprey families.

journal_name

Fish Physiol Biochem

authors

Cake MH,Potter IC,Power GW,Tajbakhsh M

doi

10.1007/BF00004649

subject

Has Abstract

pub_date

1992-05-01 00:00:00

pages

1-10

issue

1

eissn

0920-1742

issn

1573-5168

journal_volume

10

pub_type

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