Protection of Neurospora trehalase against heat inactivation

Mechanisms of protection of trehalase against heat inactivation in Neurospora.

The half-life of trehalase and invertase at 65 and 60 C was found to be much greater when intact ascospores of Neurospora tetrasperma were heated, as compared with extracts. By contrast, no protection was afforded these enzymes when they were heated in intact conidia and mycelium of N. crassa or N. tetrasperma. The protective effect of ascospores for trehalase was further investigated by heatin...

Control of trehalase synthesis in Neurospora crassa.

When an aconidial strain (STL6A) of Neurospora crassa is grown on carbon sources such as glucose, maltose, sucrose, etc., trehalase activity per unit weight of mycelium is very low. By contrast, media containing arabinose, glutamic acid, glycine, etc., which support growth only poorly, produce mycelium with very high trehalase activity. Retarding growth limiting the supply of a necessary nutrie...

Neurospora trehalase and its structural gene.

We have isolated Neurospora trehalaseless mutants and mapped the trehalase structural gene to linkage group I. The structural gene mutations not only affect thermostability and other characteristics of the enzyme but also affect the production of an inhibitor of the wild-type trehalase. The inhibitor appears to be the mutant trehalase. We suggest that the mutant subunits act as inhibitors by en...

Gonadotrophic hormone: protection against inactivation.

Protection of avian myeloblastosis virus (AMV) DNA polymerase by substrates against heat inactivation.

Purified DNA polymerase from AMV was exposed to thermal inactivation in the presence and absence of various compounds required for maximal activity. A synergistic protective effect was noted when all the components were present. The enzyme showed a distinct preference for primed templates, especially for its native 70S RNA. Heat inactivation studies also suggested that the active sites for RNas...