Differences in specificity and catalytic efficiency between allozymes of esterase-4 from Drosophila mojavensis

A more than 10-fold difference in the specificity and catalytic efficiency for 1-naphthyl esters was measured between two allozymes of esterase-4 from Drosophila mojavensis. This difference is mainly caused by a difference in the affinity for the 1-naphthyl esters. The amino acid compositions of the allozymes are not significantly different, which means that the difference in primary structure is small. Small differences in primary structure generally do not result in such a large increase in catalytic efficiency and such a large shift in substrate specificity as was found in the present study.      

Regulation of Growth in Avena Stem Segments by Gibberellic Acid and Kinetin

Kinetin at physiological concentrations causes significant reduction of GA₃-promoted growth in excised Avena stem segments. Kinetin is therefore considered to be a gibberellin-antagonist in this system. A Lineweaver-Burke plot reveals that kinetin acts non-competitively with GA₃. The kinetin inhibition of GA₃-promoted growth can be seen within 6 hours. It was found that soluble protein is markedly increased by kinetin in the tissue during the first 3 hours, thus preceding the inhibition of GA₃-promoted growth by several hours. At the cellular level, kinetin negated the blocking effect of GA₃ on cell division in the intercalary meristem portions of these segments. In fact, kinetin promotes both lateral and longitudinal cell divisions in intercalary meristem cells.