Effect of neurectomy on nuclease activity in skeletal muscles of rats

Author followed up the activity of the three enzymes involved in the catabolism of nucleic acids--acid deoxyribonulease (DNase II), alkaline ribonuclease (RNase I), and acid ribonuclease (RNase II)--in the denervated gastrocnemius and soleus muscles of rats for 28 postoperative days. The activity of both acid nucleases increased in both types of denervated muscles, compared with the respective controls. Up to the 14th postoperative day, the activity excess of both acid nucleases was more significant in the m. gastrocnemius than in the m. soleus. The RNase I ran below the control activity during the whole period in the m. soleus and up to the 14th day in the m. gastrocnemius. The role of nucleases and nuclease inhibitors in the changes of nucleic acid catabolism in neurogenic muscular atrophies is discussed.     

Microbial transformation of steroids

A systematic study of transformation reactions of Actinomycetes with respect to the progesterone molecule was undertaken. The results obtained, i.e. the types of transformation reactions in different actinomycete species, were evaluated from the point of view of taxonomy. The actinomycetes tested were divided according to the transformation types into three groups: (1) a group of species transforming progesterone in the 16α-position; (2) a group of species transforming progesterone in the β-position; (3) a group of species in which no capacity to transform progesterone into another steroid derivative was established. From the point of view of Actinomycete classification the transformation reactions on the steroid molecule fulfil all the requirements of taxonomic features of Actinomycetes. They appear to be specific properties, independent of strictly cultivation conditions and common to all the strains of individual actinomycete species tested.     

An improved glucoseoxidase--peroxidase-coupled assay for -fructofuranosidase activity

An improved glucoseoxidase-peroxidase-coupled assay for the determination of β-fructofuranosidase activity is described. The method makes use of the double effect of Tris (2-amino-2-hydroxymethylpropane-1,3-diol) as an inhibitor of both invertase and contaminating glucosidases. The method is very sensitive and is suitable for routine determinations. The total time needed for a single analysis is less than half an hour.