Maltase Glucoamylase (MGAM): Putting Diabetes in its Place! (LB85)

Isolation of a detergent-solubilized maltase/glucoamylase from rat intestine and its comparison with a maltase/glucoamylase solubilized by papain.

Maltase/glucoamylase from the rat intestinal brush-border membrane was solubilized by homogenization of the intestinal mucosa in buffer containing 0.5% Triton X-100. After removal of the detergent with butan-1-ol, the enzyme was purified by chromatography on Sepharose 4B and DEAE-cellulose. The final specific activity was 70.3 units/mg of protein in six preparations, comparing favourably with t...

Assignment of maltase glucoamylase (MGAM) gene to bovine chromosome 4q34 by in situ hybridization and confirmation by radiation hybrid mapping.

In mammals, hydrolysis of the nonreducing ends of oligosacharide chains is carried out by an enzyme complex involving sucrase-isomaltase and maltase-glucoamylase which is anchored in the mucosa of the small intestine brush border (Semenza and Aurichino, 1989). It has been hypothesized that the human MGAM activity is an alternate pathway for starch digestion when luminal ·-amylase activity is re...

Putting Hierarchy in Its Place

Putting Opacity in its Place

We clarify the relationships between Guerraoui and Kapalka’s opacity correctness condition for Transactional Memory (TM) algorithms and the TMS1 and TMS2 conditions we have previously proposed. Using formal, machine checked simulation proofs constructed using the PVS theorem proving system, we have shown that all algorithms that satisfy opacity also satisfy TMS1, and that all algorithms that sa...

Putting Liberalism in Its Place

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