Acylphosphatase increases the rate of ethanol production from glucose in cell-free extracts of Saccharomyces cerevisiae

Addition of acylphosphatase exerted a stimulating effect on the alcoholic fermentation of glucose by Saccharomyces cerevisiae. The rates of glucose degradation and ethanol production by cell-free extracts of the S-288C strain were measured in the absence and in the presence of various levels of this enzyme. Two acylphosphatase isoenzymes were used; one was purified from horse skeletal muscle and the other from human erythrocytes. Both increased the rate of alcoholic fermentation, but that from erythrocytes proved to be the more efficient. This stimulating action is probably due to an "uncoupling effect" of acylphosphatase on the fermentative process, through hydrolysis of 3-phosphoglyceroyl phosphate. This was demonstrated by the fact that alcoholic fermentation was stimulated considerably by a mixture of ADP and inorganic phosphate and by arsenate as well. The possibility of improving the fermentative capacity of microorganisms may have important biotechnological applications.     

Metacercarial dispersion and intracellular parasitism in a strigeid trematode

Combes C. and Nassi H. 1977. Metacercarial dispersion and intracellular parasitism in a strigeid trematode. International Journal for Parasitology7: 501–503. The life cycle of Apatemon graciliformis Szidat, 1928 (Trematoda, Strigeidae), a parasite of Biorrphalaria glabrata in Guadeloupe, involves a novel mode of transmission, experimentally demonstrated, between the second intermediate host and the definitive host. The furcocercariae penetrate gravid females of the ovoviviparous fish, Poecilia reticulata, and develop into metacercariae in vitelline vesicles of the embryos where they encyst a short time before parturition. The young guppies are born infected with 1–3 metacercariae. It is considered that young infected fish are more prone to predation by the definitive host, thereby increasing the probability of the cycle being completed. Domestic ducks have been experimentally infected with these metacercariae. If cercariae penetrate non-gravid P. reticulata, they enter the oocytes; this represents a phase of intracellular parasitism.     

Purification of horse muscle acylphosphatase antibodies by affinity chromatography

Horse muscle acylphosphatase antibodies were obtained by immunizing rabbits with the highly purified antigen cross-linked with glutaraldehyde. Specific antibodies were purified from the immunoglobulin fraction by affinity chromatography using a matrix coupled with the pure antigen as immunoadsorbent. The purified antibodies were partially characterized by immunodiffusion and immunoprecipitin techniques. These antibodies could be used to study aspects of the muscle acylphosphatase structure, localization and other biological properties.     

Hydrolysis by horse muscle acylphosphatase of (Ca2+ + Mg2+)-ATPase phosphorylated intermediate

Horse muscle acylphosphatase (EC 3.6.1.7) was found to hydrolyze the labeled phosphorylated intermediate of (Ca²⁺ + Mg²⁺)-ATPase from rabbit muscle. In addition, the phosphorylated peptides obtained by pepsin digestion of the labeled phosphorylated microsomes were completely hydrolyzed by acylphosphatase. These findings suggest a possible regulatory role of this enzyme in vivo on the calcium transport process by sarcoplasmic reticulum.