Isolation and characterization of two immunologically distinct forms of α-amylase and a β-amylase from seeds of germinated sorghum bicolor (L.) moench

Mundy, John (1982) Isolation and characterization of two immunologically distinct forms of α-amylase and a β-amylase from seeds of germinated sorghum bicolor (L.) moench. Carlsberg Research Communications , 47 (5). pp. 263-274.

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Abstract

Two immunologically distinct forms of or-amylase named 0t-1 and ct-2 and a 15-amylase were isolated from germinated sorghum by affinity-, hydroxylapatite- and hydrophobic interaction chromatography. The two a-amylases showed similar molecular weights of 41,500 - 42,700 as determined by electrophoresis and gel permeation chromatography. The two enzymes have similar amino acid compositions except for differences in Ser, Val, lie, and Cys. They have slightly different isoelectric points of 4.65 for ct-I (major form) and 5.1 for ct-2. at-1 and ct-2 amylases contain 0.7% and 5.7% carbohydrate by weight respectively and they exhibit different kinetic properties and substrate specificities. Crossed immunoelectrophoresis and immunodiffusion of sorghum ct-1 amylase against monospecific anti-barley ct-2 amylase showed immunological identity between barley malt a-2 and sorghum malt a-1 amylase. Non-identity was seen between sorghum ct-2 and the barley malt amylase. Sorghum ct-1 and ~t-2 amylase show partial immunological identity, a-1 amylase could only be detected in trace amounts in ungerminated sorghum.

Item Type: Article
Uncontrolled Keywords: Affinity chromatography, hydrophobic interaction, isoelectric focusing, multiple molecular forms, enzyme inhibition, monospecific antibodies
Author Affiliation: Department of Biotechnology. Carlsberg Rerearch laboratory. Gamle Carlsberg Vej 10, DK-25OO Valby Copenhagen
Subjects: Crop Improvement
Divisions: Sorghum
Depositing User: Library ICRISAT-InfoSAT
Date Deposited: 28 Mar 2012 13:58
Last Modified: 28 Mar 2012 13:59
Official URL: http://dx.doi.org/10.1007/BF02907787
URI: http://eprints.icrisat.ac.in/id/eprint/4299

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