Three forms of transketolase with differing thermal stability and affi
nity for phosphocellulose have been found in baker's yeast. They have
identical mobility in sodium dodecyl sulfate electrophoresis. Particul
ar transketolase forms from yeast, pig and rat liver, and different ra
bbit organs are similar in their thermal stability and chromatographic
behavior. The relative amounts of the isoforms appear to depend on th
e physiological state of the organism. Single crystals of the three pu
re forms were grown using ammonium sulfate precipitation and found to
differ morphologically and in stability during storage. The possibilit
y of interconversions between the enzyme forms is discussed.