PubMed HealthSearch

Biomedical subjects

A Elzanowski

Publications and source records attributed to A Elzanowski.

At least 19 recordsLinked to original sources

Homologues of catalytic domains of Cellulomonas glucanases found in fungal and Bacillus glycosidases.

We demonstrate homology between the catalytic domains of exoglucanase (1,4-beta-D-glucan cellobiohydrolase, EC 3.2.1.91) from Cellulomonas fimi and those of endoxylanases (1,4-beta-D-xylan xylanohydrolases, EC 3.2.1.8) from Bacillus sp. strain C-125 and the fungus Cryptococcus albidus; and between the catalytic domains of endoglucanase (1,4-(1,3:1,4)-beta-D-glucan 4-glucanohydrolase, EC 3.2.1.4) from Cellulomonas fimi and exoglucanase II from Trichoderma reesei. These five enzymes apparently evolved by reshuffling of two catalytic domains and several substrate-binding domains.

Actinomycetales

Cystatin domains in alpha-2-HS-glycoprotein and fetuin.

We have found that chain A of alpha-2-HS-glycoprotein contains two cystatin domains that show closest similarity to those of kininogen. Most likely, the two proteins diverged after the primary duplication of a single cystatin domain as the two cystatin domains of alpha-2-HS-glycoprotein are more similar, especially in disulfide bonding, to the corresponding domains of kininogen than to each other. We also propose that the carboxyl-terminal (non-cystatin) parts of kininogen and alpha-2-HS-glycoprotein contain homologous segments. We suggest that alpha-2-HS-glycoprotein may act as an inhibitor of the cysteine proteinases responsible for bone resorption. We have also found that fetuin is closely related to alpha-2-HS-glycoprotein.

Amino Acid Sequence

Homology of delta crystallin and argininosuccinate lyase.

1. Delta crystallin, a major lens protein characteristic of birds and reptiles, is homologous to argininosuccinate lyase; 57% of the residues in chicken delta crystallin and human lyase are identical. 2. Even more similar (62% identical residues) to the human lyase is the sequence translated from the presumably inactive delta-2 gene of the delta crystallin locus. 3. As both delta crystallin and lyase are synthesized in birds only during the embryonic and juvenile stages, the persistence of delta crystallin in the adult lens appears to be paedomorphic. 4. Possible correlations of the origins of delta crystallin with other events in sauropsid evolution are proposed.

Amino Acid Sequence

The homology of complement factor C8 gamma chain and alpha-1-microglobulin.

The sequence of the complement factor C8 gamma chain shares a remarkable degree of similarity with that of alpha-1-microglobulin, a member of the alpha-2u-globulin superfamily. This superfamily comprises a diverse group of distantly related animal proteins possessing characteristic structural features and similar functions. Comparison of the C8 gamma chain with these proteins supports its homology to them and suggests a possible functional role.

Alpha-Globulins