Linked Life Data

3343970

Source:http://linkedlifedata.com/resource/pubmed/id/3343970

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-3-30
pubmed:abstractText
Many biological properties of immune complexes (IC) depend upon their size. Quasi-elastic light scattering (QLS) was used to measure a mean equivalent hydrodynamic radius (Rh) and variance of the distribution of model IC composed of bovine serum albumin (BSA) as antigen (Ag) and combinations of two or three well-characterized monoclonal antibodies (MAb) which bound noncompetitively to unique epitopes on BSA. With the molar ratio (X) of each MAb to Ag fixed, Rh increased with concn. Rh was maximal at equivalence (X = 0.5) with two MAb and at slight MAb excess (X = 0.67) with three MAb. The largest Rh with two MAb was about 200 A, and Rh was uniformly different amongst the three combinations of two MAb IC. The largest hydrodynamic radius of individual complexes which formed with two MAb was estimated to be about 400 A; even larger individual complexes were formed with three MAb. Size changes following alteration of solution concns were also followed with QLS. Kinetics of two MAb IC association were too fast to observe; dissociation following large dilution (40-fold) required 5-10 min to attain a new steady state, much less at small dilution. With three MAb, Rh dropped sharply in 5 min and became steady after 1-2 hr. These results suggest that conventional chromatographic and ultracentrifugation techniques for studying IC size, involving large dilution and long measurement time, provide misleading results. Association of three MAb produced a rapid initial increase of Rh in several min, followed by diverse behavior which depended upon concn. From high to low concn, these included (1) exponential growth of Rh with time and appearance of visible macroscopic particles; (2) metastable states for several hr followed by slow growth to large size over several days, leading to formation of particles; and (3) rapid growth to steady state conditions with no visible particles. This heretofore unobserved equilibrium and kinetic behavior of model IC in solution may be reflected in the behavior of more complex, naturally occurring IC.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17-32
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Quasi-elastic light scattering of antigen-antibody complexes.
pubmed:affiliation
Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge 02139.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't