Search

The N‐terminal amino acid sequences of two chloroform/methanol soluble globulins from barley and one form wheat are reported. They are homologous with N‐terminal sequences previously reported for α‐amylase and trypsin inhibitors from cereals and 2 S storage proteins from castor bean and rape. Three albumins were also purified from Aegilops squarrosaand Triticum monococcum. These had N‐terminal amino acid sequences most closely related to the α‐amylase and trypsin inhibitors. The relationships of this superfamily of seed proteins are discussed.

A tetrameric inhibitor that is active against α‐amylase from the larvae of the insect Tenebrio molitor, but inactive against the enzyme from human saliva and against the endogenous one, has been described in barley endosperm. The subunits of the inhibitor have been identified as the previously characterized proteins CMa, CMb and CMd, of which only CMa was inhibitory by itself.

A barley salt-soluble protein of 14.5 kDa, which inhibits the α-amylase from the insect Tenebrio molitor, has been identified as a major IgE-binding component of sera from baker's asthma patients. The N-terminal amino acid sequence of this protein indicates that it is a member of a previously described family of α-amylase/trypsin inhibitors.