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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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書目詳細資料
發表在:Infect Immun
Main Authors: Maynard, M T, Kuramitsu, H K
格式: Artigo
語言:Inglês
出版: American Society for Microbiology (ASM) 1979
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在線閱讀:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC414244/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/457262/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/iai.23.3.873-883.1979
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