Structure of human salivary alpha-amylase crystallized in a C-centered monoclinic space group.

ABSTRACT: Human salivary alpha-amylase (HSA) is a major secretory protein component of saliva and has important biological functions, including the initial digestion of starch. HSA acts as a monomer and mediates the hydrolysis of alpha-1,4-glucosidic linkages in oligosaccharides. To date, all published crystal structures of HSA have been crystallized as monomers in space group P2(1)2(1)2(1). Here, the serendipitous purification, crystallization and ultimate structure determination of a HSA non-crystallographic symmetry (NCS) dimer, while attempting to purify human carbonic anhydrase VI (HCA VI) from saliva using an affinity resin for alpha-class carbonic anhydrases, is presented. On further investigation, it was shown that HSA could only be copurified using the affinity resin in the presence of HCA

SUBMITTER: Fisher SZ 

PROVIDER: S-EPMC2150953 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature