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1 ity seeds)--the natural sources of ricin and abrin.
2 toxication operated by type 2 RIPs ricin and abrin.
3 whose B chains are believed to either have (abrin-a and abrin-d) or lack (abrin-b and abrin-c) the a
5 ant protein that occurs in several isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains a
6 od and clinical matrices for the isoforms of abrin and also the closely related, less toxic Abrus pre
9 resistant to the Gal-binding lectins ricin, abrin, and modeccin and hypersensitive to the toxicity o
11 tivating proteins (RIPs) family (e.g. ricin, abrin) are potent cytotoxins showing a strong lethal act
13 in that occurs in several isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains are believ
14 ccurs in several isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains are believed to eit
16 preproabrin cDNA, tentatively identified as abrin-c, which was predicted to lack lectin activity, an
17 resulted in a dramatic increase of ricin or abrin cytotoxicity compared with control mock-treated ce
18 ins are believed to either have (abrin-a and abrin-d) or lack (abrin-b and abrin-c) the ability to bi
19 eral isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains are believed to either have (ab
22 t enhanced the activities of ricin, RCA, and abrin II to different extents, thus improving the diagno
27 ted with magnetic beads coated with multiple abrin-specific antibodies, thereby concentrating and ext
29 -II family of plant proteins, such as ricin, abrin, viscumin, and volkensin was based on their affini
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