rat tapeworm (Hymenolegsis diminuta) catalyzes hydrogen in transfer
from NADPH to NAD, producing NADH. This enzyme is known to serve a
vital role in the tapeworm’s anaerobic metabolism, and it has
recently been hypothesized that it may serve as a proton exchange
pump, transferring protons across the mitochondrial membrane. A
study on “Effect of Various Substrate Concentrations on the
Conformational Variation of the NADPH: NAD Transhydrogenase of
Hymenolepsis Diminuta” conducted in 1983 at Bowling Green State
University was designed to assess the ability of this enzyme to
undergo conformation or shape changes. Changes in the specific
activity of the enzyme caused by variations in the concentration of
NADP could be interpreted as supporting the theory of
conformational change. The enzyme in question is located in the
inner membrane of the tapeworm’s mitochondria. These tapeworms were
homogenized, and through a series of centrifugations, the enzyme
was isolated. Various concentrations of NADP were then added to the
isolated enzyme solution, and the mizture was then incubated in a
water bath at 560C for 3 minutes. The enzyme was then analyzed on
dual beam spectrophotometer, and the following resultswere
calculated in terms of the specific gravity of the enzyme in
nanomoles per minute per milligram of protein:
- The Mitochondrial Enzyme Naph Nad Transhydrogenase Of The Common Rat Tapeworm Hymenolegsis Diminuta Catalyzes Hydrogen 1 (31.41 KiB) Viewed 31 times