An investigation of the cranial evolution of Asian pitvipers (Serpentes: Crotalinae), with comments on the phylogenetic position of Peltopelor macrolepis

Guo, P., Jadin, R.C., Malhotra, A. and Li, C. 2009. An investigation of the cranial evolution of Asian pitvipers (Serpentes: Crotalinae), with comments on the phylogenetic position of Peltopelor macrolepis—Acta Zoologica (Stockholm) 91 : 402–407. We investigated the evolution of 12 cranial characters of 31 species of Asian pitvipers by examining the character state changes on a consensus tree modified from broadly consistent molecular results. We found that these characters appear stable with only one intraspecific polymorphism. Nine of the 12 characters form useful synapomorphies, whereas three are ambiguous and evolutionarily plastic. Clades that are supported with numerous apomorphies are the Trimeresurus group [consisting of the recently defined genera Trimeresurus sensu Malhotra and Thorpe (2004) , Parias, Popeia, Viridovipera, Himalayophis, and Cryptelytrops] and the genera Protobothrops, Parias, and Viridovipera. Two species previously considered as congeners but now known to be distantly related, Ovophis monticola and ‘Ovophis’okinavensis, have nearly identical character states, demonstrating substantial convergence in cranial characters. Finally, we attempt to infer the phylogenetic position of Peltopelor macrolepis by comparing its cranial features with that of other pitvipers.     

Steady-state kinetic properties of phosphoglycerate kinase of mung beans

Steady-state kinetics of the action of mung bean phosphoglycerate kinase have been investigated using 3-phosphoglycerate and ATP as substrates in the presence of Mg2+ ions. Keeping a constant and high Mg2+ concentration and varying the concentration of one of the substrates (ATP or 3-phosphoglycerates) at several fixed concentrations of the other substrate (3-phosphoglycerate or ATP), the Km values of Mg.ATP2- and 3-phosphoglycerate were found to be 0.42 and 0.60 mM, respectively. These values are independent of the concentration of the other substrate. A limiting value of Vmax, where the enzyme is saturated with both the substrates, was found to be 39.4 mumoles product formed per min per mg enzyme protein. This corresponds to a turnover number equal to 31.5 sec-1 (for molecular weight of the enzyme equal to 48,000). If [Mg2+] and [ATP4-] are held equal and varied together at several fixed concentrations of 3-phosphoglycerate, deviations from Michaelis-Menten kinetics (non-linear Lineweaver-Burk plots) are observed at lower values of ATP4- and Mg2+ (less than 0.1 mM), giving rise to apparent sigmoidicity in the rate versus [ATP4-] plots. It has been suggested that the real substrate for this enzyme is the Mg.ATP2- complex (and not free ATP4-). The complex dissociates at lower values of [Mg2+] and [ATP4-]. The resulting disproportionate decrease in the concentration of the complex brings about a steeper fall in the rate of reaction than is required by the Michaelis-Menten equation, giving rise to an apparent sigmoidicity.(ABSTRACT TRUNCATED AT 250 WORDS)