Proteolytic specificity of rhodostoxin, the major hemorrhagin of Calloselasma rhodostoma (Malayan pit viper) venom
Toxicon, ISSN: 0041-0101, Vol: 35, Issue: 6, Page: 979-984
1997
- 11Citations
- 13Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations11
- Citation Indexes11
- 11
- CrossRef7
- Captures13
- Readers13
- 13
Article Description
The proteolytic specificity of rhodostoxin, the major hemorrhagin from Calloselasma rhodostoma (Malayan pit viper) venom was investigated using oxidized B-chain of bovine insulin as substrate. Six peptide bonds were cleaved: Ser 9 -Hist 10, His 10 -Leu 11, Ala 14 -Leu 15, Tyr 16 -Leu 17, Gly 20 -Glu 21 and Phe 24 -Phe 25. Deglycosylated rhodostoxin, however, cleaved primarily at Arg 22 -Gly 23.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0041010196001869; http://dx.doi.org/10.1016/s0041-0101(96)00186-9; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0031172516&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9241791; http://linkinghub.elsevier.com/retrieve/pii/S0041010196001869; http://api.elsevier.com/content/article/PII:S0041010196001869?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0041010196001869?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0041010196001869; http://dx.doi.org/10.1016/s0041-0101%2896%2900186-9; https://dx.doi.org/10.1016/s0041-0101%2896%2900186-9
Elsevier BV
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