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Two distinct secretory ribonucleases from human cerebrum: purification, characterization and relationships to other ribonucleases.

Two RNAases from human cerebrum were purified to an electrophoretically homogeneous state and their molecular masses were 22.0 kDa (tentatively called RNAase HB-1) and 19.0 kDa (RNAase HB-2). Analyses of the amino acid compositions, N-terminal amino acid sequences and catalytic properties of these e...

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Detaylı Bibliyografya
Asıl Yazarlar: Yasuda, T, Nadano, D, Takeshita, H, Kishi, K
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1993
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1137742/
https://ncbi.nlm.nih.gov/pubmed/8280059
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