Sub-Coulomb (d,p) stripping on theN=82isotones

The Preparation and Properties of Triosephosphate Isomerase from Chicken Muscle and a Comparison with that from Rabbit Muscle

“…2000 obtained by Norton et al [2] for. rabbit muscle triosephosphate isomerase agrees well with the value reported here but was the mean of only three The molecular weight of 53000 experiments.…”

“…Values for the native molecular weight of rabbit muscle triosephosphate isomerase obtained prior to 1970 are summarised by Norton et al [2] and range from 43000 to 60000. To these must be added the values of 56000-60000 obtained by Krietsch et al [3] and of 44000-49000 obtained by Lee et al [4].…”

“…simple and yields a homogeneous product as judged by electrophoresis on polyacrylamide gels a t pH 8.5 and 9.5. The gels a t pH 8.5 were capable of resolving chicken muscle triosephosphate isomerase from the rabbit muscle enzyme which itself appeared to be homogeneous, in contrast 1 o the reported heterogeneity of commercial preparations [2]. The molecular weight of the chicken muscle enzyme was measured by equilibrium sedimentation and the close agreement of the two molecular weight averages ( M , and M z ) is a proof of the monodispersity of the preparation with respect to molecular weight.…”

“…Estimates of the subunit molecular weights of the two enzymes were also obtained by electrophoresis on polyacrylamide gels containing sodium dodecylsulphate. The values of 26000 obtained for the rabbit muscle enzyme by this method and of 25 700 by equilibrium sedimentation are in close agreement with the values of 26500 quoted by Coulson et al [22] and Norton et al [2], as obtained by this gel method.…”

“…The enzyme triosephosphate isomerase plays a central role in glycolysis. I n recent years interest has centred on the enzyme obtained from rabbit muscle and preparative procedures have been described by Czok and Bucher {I] and Norton et al [2]. These last authors and also Krietsch et al [3] and Lee et al [4] have studied the molecular weight of the enzyme without, however, direct determinations of the partial specific volumes, and considerable evidence has been presented to show that the native enzyme is composed of two subunits [2,3,5-91. The enzyme obtained from chicken muscle is also of interest and work is in progress on its amino acid sequence [lo] and on its high-resolution crystal structure [ll].…”