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Purification and characterization of a metallo-endoproteinase from mouse kidney.

A metallo-endoproteinase was purified from mouse kidney. The enzyme was solubilized from the 100 000 g sediment of kidney homogenates with toluene and trypsin, and further purified by fractionation with (NH4)2SO4. DEAE-cellulose chromatography and gel filtration. The molecular weight of the metallop...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Beynon, R J, Shannon, J D, Bond, J S
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 1981
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC1163414/
https://ncbi.nlm.nih.gov/pubmed/7041888
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