Alpha -Glucosidase activity in haemolymph of the American cockroach, Periplaneta americana

Matthews, J.R.; Downer, R.G.H.; Morrison, P.E.

Journal of Insect Physiology 22(1): 157-163

1976


ISSN/ISBN: 0022-1910
Accession: 000579813

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Abstract
The alpha -glucosidase activity of whole haemolymph was investigated in adult males of Periplaneta americana (L.). Two electrophoretically distinguishable enzymes capable of hydrolysing alpha -glucosidic linkages were present in the serum component of the haemolymph, and one of these hydrolysed trehalose. Trehalase activity was also present in haemocytes, and the haemocyte enzyme shared an identical electrophoretic mobility and similar pH sensitivity with the serum trehalase. Furthermore, both enzymes were inhibited to the same extent by sodium ethylenediamine-tetraacetate (EDTA); thus, it is suggested that the same enzyme may be responsible for trehalase activity in the two components. The Km of EDTA-inhibited trehalase was 3.3 mM and this value was reduced to 1.8 mM on activation of the enzyme by calcium ions. The properties of the trehalase are discussed in light of the possible role of the enzyme in regulating haemolymph trehalose and glucose concentrations.