Linked Life Data

3942745

Source:http://linkedlifedata.com/resource/pubmed/id/3942745

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-3-21
pubmed:abstractText
The binding of the crustacean-selective protein neurotoxin, toxin B-IV, from the heteronemertine Cerebratulus lacteus, to lobster axonal and muscle membranes has been studied. Synthesis of a radioactive bifunctional cross-linking reagent, 125I-azidosalicylic acid (ASA) B-IV, has allowed these studies as well as experiments that show cross-linking of toxin B-IV to its receptor in axonal membranes. In the absence of photolysis 125I-ASA-B-IV binds to vesicles with an apparent Kd of 30 nM and maximal binding of 7.5 pmol per mg membrane protein. Photolysis of the toxin-receptor complex at 366 nm greatly diminishes the rate of dissociation of bound toxin B-IV. Photolysis also results in the specific cross-linking to axonal proteins of molecular masses 38 and 40 kDa. This cross-linking is not observed in the presence of micromolar unlabeled toxin, in the absence of photolysis or in the presence of 150 mM K+. There is no evidence of cross-linking to proteins of higher molecular weight. The radiolabeled toxin B-IV was also found to bind to lobster muscle membranes with a dissociation constant of 500 nM and a maximum binding of approx. 4.50 pmol per mg membrane protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
855
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Structure and action of heteronemertine polypeptide toxins. Specific cross-linking of Cerebratulus lacteus toxin B-IV to lobster axon membrane vesicles.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.