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Glutamate 1-semialdehyde aminotransferase has been separated from metabolically related activities by gel filtration and affinity chromatography. The enzyme was inhibited by gabaculin, 4-amino 5-fluoropentanoic acid and pyridoxal 5-phosphate and stimulated by pyridoxamine 5-phosphate. The activity of enzyme recovered by elution after electrophoresis in non-denaturing polyacrylamide gels was wholly dependent on pyridoxamine 5-phosphate. A mechanism for the enzyme-catalysed reaction based on these observations is discussed.

A small basic 10 kD abundant protein in barley seeds can convey up to 7% of the phosphatidylcholine in liposomes to potato mitochondria whereas cholesteryloleate is not transported. The demonstration of this activity combined with a somewhat more than 50% homology of its primary structure to that of other plant phospholipid transfer proteins are the bases for our naming it a barley lipid transfer protein (LTP).