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Purification and antigenic properties of intracellular invertase from Streptococcus mutans.

Intracellular invertase from Streptococcus mutans GS5 was purified to near homogeneity by gel filtration and ion-exchange chromatography followed by preparative polyacrylamide gel electrophoresis. The invertase appeared to be composed of a single polypeptide chain with a molecular weight of 48,000....

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Dettagli Bibliografici
Autori principali: Maynard, M T, Kuramitsu, H K
Natura: Artigo
Lingua:Inglês
Pubblicazione: 1979
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC414244/
https://ncbi.nlm.nih.gov/pubmed/457262
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