Novel cold-adapted raw-starch digesting α-amylases from : Gene cloning, expression, and characterization.

We identified the raw-starch-digesting α-amylase genes a earthworm and ( and ). Each gene consists of 1,530 base pairs (bp) that encode proteins of 510 amino acids, as indicated by the corresponding mRNA sequences. Ef-Amy I and II showed an 89% amino acid identity.

X-ray crystallographic structural studies of α-amylase I from Eisenia fetida.

The earthworm Eisenia fetida possesses several cold-active enzymes, including α-amylase, β-glucanase and β-mannanase. E. fetida possesses two isoforms of α-amylase (Ef-Amy I and II) to digest raw starch.

Enzymatic characterization of germination-specific cysteine protease-1 expressed transiently in cotyledons during the early phase of germination.

Papain-like cysteine protease activity that shows a unique transient expression profile in cotyledons of daikon radish during germination was detected. The enzyme showed a distinct elution pattern on DEAE-cellulose compared with cathepsin B-like and Responsive to dessication-21 cysteine protease. Although this activity was not detected in seed prior to imbibition, the activity increased markedly and reached a maximum at 2 days after imbibition and then decreased rapidly and completely disappeared after 5 days.

Interleukin-10 promoter gene polymorphisms have no clear influence on interleukin-10 protein secretion in AIDS-associated B-cell lines.

Interleukin-10 (IL-10) is a pleiotropic cytokine involved in several immune responses and expressed by a variety of cell types. IL-10 interacts with at least two subunits of the IL-10 receptors (IL-10R1 and IL-10R2), which are members of the interferon receptor family, and play important roles in ligand binding and signaling. Using reverse transcriptase-polymerase chain reaction (RT-PCR) and enzyme-linked immunosorbent assay (ELISA) methods, the mRNA expression and secretion patterns of IL-10 were studied.