| Autor: |
S, Gulnik, E T, Baldwin, N, Tarasova, J, Erickson |
| Rok vydání: |
1992 |
| Předmět: |
|
| Zdroj: |
Journal of molecular biology. 227(1) |
| ISSN: |
0022-2836 |
| Popis: |
The two-chain form of active cathepsin D, a glycosylated, lysosomal aspartic proteinase, has been isolated from human liver. Isoelectric focusing revealed two major species of enzyme that differed by approximately 0.2 pI unit. Crystals suitable for X-ray diffraction analysis were prepared from acidic solutions using precipitation with ammonium sulfate. The hexagonal crystals diffracted X-rays to beyond 3.1 A resolution and belonged to space group P6(1) (or P6(5)) with cell constants a = b = 125.9 A, c = 104.1 A, gamma = 120.0 degrees. The crystals likely contain two molecules in the asymmetric unit, giving a solvent content of 56% (v/w). Biochemical analysis of crystals indicated that both isoforms were present in approximately equimolar proportions. Full structure determination of the enzyme is underway. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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