The A-hordeins as a group of salt soluble hydrophobic proteins

Morocco as a possible domestication center for barley: biochemical and agromorphological evidence

“…Figure 1 is a composite diagram where the relative positions of all the variants are shown in the 2-dimensional map. The CM-proteins are low molecular weight, salt-soluble hydrophobic polypeptides that are selectively extracted from barley endosperm with chloroform: methanol 2:1 (v/v) (Salcedo et al 1980). The standard phenotype, that of 'Zephyr' barley, consists of 5 components: CMa-1, CMb-1, CMc-1, CMd-1 and CMe-1 (Fig.…”

“…In our survey, we have investigated the genetic variability of the CM-proteins, which are the main components of the A-hordeins (Salcedo et al 1980(Salcedo et al , 1982. The A-hordeins are less variable both in the cultivated and in the wild species than the B-, C-and D-hordeins (Dolí and Brown 1979;Shewry et al 1979Shewry et al , 1983 and are, therefore, more suitable biochemical markers in phylogenetical studies.…”

In vivo and in vitro synthesis of CM-proteins (A-hordeins) from barley (Hordeum vulgare L.)

“…The B-and C-hordeins have been characterized as storage proteins, located in the protein bodies, and have been found to be controlled by two linked loci, Hord-2 and Hord-1, respectively (Dolí and Brown 1979;Shewry et al 1980a). The function of the A-hordeins is unclear and it has been suggested that they are not located in the protein bodies (Holder and Ingversen 1978;Salcedo et al 1980). Recent studies from this laboratory have shown that the main components of this fraction are not true prolamins because they are soluble in aqueous buffers and their amino acid compositions are atypical, although, as with the prolamins, they are soluble in aqueous alcohols and in chloroform:methanol mixtures (Salcedo et al 1980;Aragoncillo et al 1981;Salcedo et al 1982).…”

“…The function of the A-hordeins is unclear and it has been suggested that they are not located in the protein bodies (Holder and Ingversen 1978;Salcedo et al 1980). Recent studies from this laboratory have shown that the main components of this fraction are not true prolamins because they are soluble in aqueous buffers and their amino acid compositions are atypical, although, as with the prolamins, they are soluble in aqueous alcohols and in chloroform:methanol mixtures (Salcedo et al 1980;Aragoncillo et al 1981;Salcedo et al 1982). It has also been shown that they are homologous to the wheat and rye CM-proteins, and possibly to similar proteins present in other Gramineae, so it has been proposed that the designation of CM-proteins be extended to the four components purified from barley (CMa, b, c, and d) (Salcedo et al 1982;Paz-Ares et al, in press).…”

Genetics of CM-proteins (A-hordeins) in barley

“…At least two subgroups of proteins have been described within the A-hordein fraction, namely the CM-proteins, which include the main components, and the low-molecular-weight hordeins (Salcedo et al 1980;Aragoncillo et al 1981;Salcedo etal. 1982;PazAres et al 1983 a).…”