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Publikováno v:
Journal of Biological Chemistry. 276:12434-12439
Factor VIII circulates as a noncovalent heterodimer consisting of a heavy chain (HC, contiguous A1-A2-B domains) and light chain (LC). Cleavage of HC at the A1-A2 and A2-B junctions generates the A1 and A2 subunits of factor VIIIa. Although the isola
Autor:
Gertraud Feldmaier-Fuchs, Thorsten Schweikardt, Renate Voit, Heinz Decker, Thorsten Burmester
Publikováno v:
Journal of Biological Chemistry. 275:39339-39344
Hemocyanins are large oligomeric respiratory proteins found in many arthropods and molluscs. The hemocyanin of the tarantula Eurypelma californicum is a 24-mer protein complex with molecular mass of 1,726,459 Da that consists of seven different polyp
Autor:
Heinz Decker, Thomas Rimke
Publikováno v:
Journal of Biological Chemistry. 273:25889-25892
An enzyme generally catalyzes one well defined reaction with high specificity and efficiency. We report here in contrast that the copper protein hemocyanin of the tarantula Eurypelma californicum exhibits two different functions. These occur at the s
Autor:
Yu Feng, Michael Forgac
Publikováno v:
Journal of Biological Chemistry. 267:5817-5822
The vacuolar class of (H+)-ATPases are highly sensitive to sulfhydryl reagents, such as N-ethylmaleimide. The cysteine residue which is responsible for inhibition of the coated vesicle (H+)-ATPase upon modification by N-ethylmalemide is located in su
Publikováno v:
Journal of Biological Chemistry. 267:60-65
Structural analogs of recombinant human insulin-like growth factor-I (IGF-I), with alterations to each of the B, C, A, and D domains, have been tested for their ability to form binary complexes with IGF-binding protein-3 (IGFBP-3) and ternary complex
Publikováno v:
Journal of Biological Chemistry. 266:20139-20145
Human factor VIII and factor VIIIa were proteolytically inactivated by activated protein C. Cleavages occurred within the heavy chain (contiguous A1-A2-B domains) of factor VIII and in the heavy chain-derived A1 and A2 subunits of factor VIIIa, where
Publikováno v:
Journal of Biological Chemistry. 266:4187-4193
In porcine cytosolic aspartate aminotransferase, a dimeric enzyme, the amino-terminal region anchoring onto the neighboring subunit is linked to the adjoining floppy peptide segment (residues 12-47), an integral part of the small domain whose facile
Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the alpha subunit
Publikováno v:
Journal of Biological Chemistry. 265:4204-4209
Bacillus subtilis has two different riboflavin synthases characterized by the subunit structures alpha3 (light enzyme) and alpha3beta60 (heavy enzyme). The light enzyme was purified by a novel procedure with increased yield and excellent reproducibil
Publikováno v:
Journal of Biological Chemistry. 265:3726-3730
Using the Tb3+ luminescence technique, we showed that bovine subunit III, a defective pancreatic serine endopeptidase-like protease, possessed a single metal ion binding site able to bind Tb3+ with a high affinity comparable to that of porcine elasta
Autor:
B R DasGupta, V Sathyamoorthy
Publikováno v:
Journal of Biological Chemistry. 260:10461-10466
Clostridium botulinum produces botulinum neurotoxin (NT) in antigenically distinct forms. When isolated from bacterial cultures type E is a single chain, type B is a mixture of single and two-chain molecules, and type A is essentially a two-chain mol