Calorimetric studies on the stability of the ribosome-inactivating protein abrin II: effects of pH and ligand binding.

The effects of pH and ligand binding on the stability of abrin II, a heterodimeric ribosome-inactivating protein, and its subunits have been studied using high-sensitivity differential scanning calorimetry. At pH7.2, the calorimetric scan consists of two transitions, which correspond to the B-subuni...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Krupakar, J, Swaminathan, C P, Das, P K, Surolia, A, Podder, S K
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 1999
Aiheet:
Research Article
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC1220052/
https://ncbi.nlm.nih.gov/pubmed/10024502
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