(full paper is archived in the Miller Library)
Title: Laminarinase and hexokinase activity during embryonic development of Acmaea scutum (Mollusca: Gastropoda)
Student Author(s): Muchmore, Andrew V.
Faculty Advisor(s): Epel, David
Location: Final Papers Biology 175H
Date: June 1966
Abstract: Activity of embryonic carbohydrases, hexokinase, glucose-6-phosphate dehydrogenase, and isocitrate dehydrogenase were analyzed fluormetrically in the unfertiliaed eggs, trochophores, and veligers of the limpet Acmaea scutum. Glucose-6-phosphate and isocitrate dehydrogenase activity were constant at all stages. Hexokinase activity increased almost three-fold between the trochophore and veliger stage. No maltase, galactosidase, or amylase activity was found at any stage. A laminarinase-type enzyme, capable of degrading algal laminarin to free glucose, was found in all embyronic stages. This enzyme may be involved in digestion of laminarin when the embryo becomes a feeding larvae, or may be involved in intracellular breakdown of beta, 1-3 linked glycoproteins during embryogenesis.
Notes: Published 1968, Veliger 11(Suppl): 105-108