Biomedical subjects

V Puizdar

Publications and source records attributed to V Puizdar.

3 recordsLinked to original sources

PubMed1986

Structural differences between rabbit cathepsin E and cathepsin D.

Rabbit cathepsins D and E were isolated from bone marrow. Both enzymes were purified by affinity chromatography on pepstatin-Sepharose 4B and Con A-Sepharose 4B. Purity of the enzymes was ascertained by two-dimensional gel electrophoresis after iodination. The isoelectric point of cathepsin D was found to be 6.95. Cathepsin E was shown to consist of two subunits having molecular masses each of 40 kDa and isoelectric points of 4.60 and 4.65, respectively. The amino-acid composition of cathepsin E was found to be different from that of cathepsin D.

Amino Acids↗

PubMed1985

Evidence for the presence of large amounts of cathepsin E in rat spleen.

Although cathepsin E is present in trace amounts in spleen from several species, it was found in large amounts in rat spleen. This observation can be correlated with the fact that spleen in the rat is an important organ in haemopoeisis.

Animals↗

PubMed1982

Aspartic proteinases: their activation and structural studies.

Besides extracellular mammalian aspartic proteinases also intracellular proteinase cathepsin D is synthesized in the form of a precursor. The evidence is presented that cathepsin D zymogen (cathepsinogen D, procathepsin D) can be activated by a similar mechanism to that of pepsin, releasing an activation segment - peptide(s). The released peptide(s) show inhibitory activity towards cathepsin D and some other aspartic proteinases. The activation peptides released from bovine pepsinogen do not inhibit cathepsins D and E. The structure of different aspartic proteinases was studied by circular dichroism measurements. The binding of pepstatin causes conformational changes in the near UV CD spectrum.

Amino Acids↗