Linked Life Data

2663154

Source:http://linkedlifedata.com/resource/pubmed/id/2663154

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-8-25
pubmed:abstractText
The immunochemical properties between phospho-D-mannan-protein complexes of yeast (Y) and mycelial (M) forms of Candida albicans NIH A-207 (serotype A) strain were compared. Hydrolysis of the Y-form complex gave a mixture of beta-(1----2)-linked D-mannooligosaccharides consisting mainly of tri- and tetra-ose, whereas the M-form complex gave preponderantly D-mannose. The antiserum against Y-form cells exhibited a lower reactivity with the M-form than with the Y-form complex, whereas the antiserum to M-form cells could not distinguish significantly between both complexes. Moreover, these acid-modified complexes showed lower antibody-precipitating effect than each corresponding intact complex against antisera of Y- and M-form cells. Digestion of the acid-modified Y- and M-form complexes with the Arthrobacter GJM-1 strain alpha-D-mannosidase yielded 35- and 40-% degradation products, respectively. Acetolysis of each modified complex under mild conditions gave the same D-mannohexaose, beta-D-Manp-(1----2)-beta-D-Manp-(1----2)-alpha-D-Manp -(1----2)-alpha-D-Manp- (1----2)-alpha-D-Manp-(1----2)-D-Man. Because the complexes of Y- and M-form cells of C. albicans NIH B-792 (serotype B) strain did not give any hexaose fraction containing beta-(1----2) linkages, the presence of this hexaose can be regarded as one of the dominant characteristics of the serotype-A specificity of C. albicans spp.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0008-6215
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
187
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
239-53
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Structural analysis of phospho-D-mannan-protein complexes isolated from yeast and mold form cells of Candida albicans NIH A-207 serotype A strain.
pubmed:affiliation
Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Sendai, Japan.
pubmed:publicationType
Journal Article, Comparative Study