scholarly journals An unsulphated region of the rat chondrosarcoma chondroitin sulphate chain and its binding to monoclonal antibody 3B3

1991 ◽  
Vol 273 (1) ◽  
pp. 237-239 ◽  
Author(s):  
J R Baker ◽  
J E Christner ◽  
S L Ekborg
Keyword(s):  
Monoclonal Antibody ◽  
Structure Function ◽  
Chondroitin Sulphate ◽  
Significant Proportion ◽  
Physiological Significance ◽  
High Concentration ◽  
Chondroitinase Abc ◽  
Linkage Region ◽  
Unsaturated Disaccharide ◽  
Chondroitin Sulphate Chain

The chondroitin sulphate chains of proteoglycans are not uniformly sulphated. Commonly, regions of under- and over-sulphation are found. It is probable that variability in chondroitin sulphation has physiological significance, although such structure-function relationships largely remain unexplored. Chondroitin sulphate from rat chondrosarcoma proteoglycan has been found to possess no oversulphated residues. It is primarily chondroitin 4-sulphate, although a significant proportion of unsulphated disaccharides (14%) are also present. It appears that some unsulphated disaccharides are concentrated only at the point of attachment to the linkage region (i.e. it is the major unsaturated disaccharide remaining attached to chondrosarcoma proteoglycan core produced by chondroitinase ABC digestion). This proteoglycan core binds monoclonal antibody (MAb) 3B3. Although 3B3 principally binds to 6-sulphated ‘stubs’ of proteoglycan cores [Couchman, Caterson, Christner & Baker (1984) Nature (London) 307, 650-652], given a high concentration of unsulphated ‘stubs’, it can alternatively bind to these residues. It is also evident that caution must be exercised in using MAb 3B3 to identify chondroitin 6-sulphated proteoglycans.

scholarly journals The distribution of sulphate residues in the chondroitin sulphate chain

1971 ◽  
Vol 125 (3) ◽  
pp. 903-908 ◽  
Author(s):  
Åke Wasteson ◽  
Ulf Lindahl
Keyword(s):  
Chondroitin Sulphate ◽  
Gel Chromatography ◽  
Neutral Sugar ◽  
Charge Heterogeneity ◽  
Linkage Region ◽  
Molar Ratios ◽  
Before And After ◽  
Dowex 1 ◽  
Chondroitin Sulphate Chain ◽  
Testicular Hyaluronidase

1. Electrophoresis of chondroitin sulphate, before and after partial degradation with testicular hyaluronidase, revealed charge heterogeneity of the degraded but not of the intact polymer. 2. Hyaluronidase-treated chondroitin sulphate was fractionated by gel chromatography. Two subfractions which were essentially monodisperse with regard to molecular weight (values of 8600 and 4800, respectively) were separated further by chromatography on Dowex 1. The resulting subfractions differed considerably with respect to their sulphate/disaccharide molar ratios. 3. Amino acid and neutral-sugar analyses of the Dowex 1 subfractions showed that the less sulphated fragments contained the carbohydrate–protein linkage region, whereas the high-sulphated fragments essentially lacked this constituent. It was concluded that chondroitin sulphate contains relatively less sulphate in the vicinity of the carbohydrate–protein linkage region than in the more peripheral portion of the polysaccharide chain.

scholarly journals Primitive hematopoietic cells in murine bone marrow express the CD34 antigen

Blood ◽  
1996 ◽  
Vol 88 (10) ◽  
pp. 3774-3784 ◽  
Author(s):  
F Morel ◽  
SJ Szilvassy ◽  
M Travis ◽  
B Chen ◽  
A Galy
Keyword(s):  
Stem Cells ◽  
Monoclonal Antibody ◽  
Bone Marrow ◽  
Progenitor Cells ◽  
Significant Proportion ◽  
Hematopoietic Cells ◽  
Full Detail ◽  
Hematopoietic Stem ◽  
Cd34 Antigen

The CD34 antigen is expressed on most, if not all, human hematopoietic stem cells (HSCs) and hematopoietic progenitor cells, and its use for the enrichment of HSCs with repopulating potential is well established. However, despite homology between human and murine CD34, its expression on subsets of primitive murine hematopoietic cells has not been examined in full detail. To address this issue, we used a novel monoclonal antibody against murine CD34 (RAM34) to fractionate bone marrow (BM) cells that were then assayed in vitro and in vivo with respect to differing functional properties. A total of 4% to 17% of murine BM cells expressed CD34 at intermediate to high levels, representing a marked improvement over the resolution obtained with previously described polyclonal anti-CD34 antibodies. Sixty percent of CD34+ BM cells lacked lineage (Lin) markers expressed on mature lymphoid or myeloid cells. Eighty-five percent of Sca-1+Thy-1(10)Lin- /10 cells that are highly enriched in HSCs expressed intermediate, but not high, levels of CD34 antigen. The remainder of these phenotypically defined stem cells were CD34-. In vitro colony-forming cells, day-8 and -12 spleen colony-forming units (CFU-S), primitive progenitors able to differentiate into B lymphocytes in vitro or into T lymphocytes in SCID mice, and stem cells with radioprotective and competitive long-term repopulating activity were all markedly enriched in the CD34+ fraction after single-parameter cell sorting. In contrast, CD34-BM cells were depleted of such activities at the cell doses tested and were capable of only short-term B-cell production in vitro. The results indicate that a significant proportion of murine HSCs and multilineage progenitor cells express detectable levels of CD34, and that the RAM34 monoclonal antibody is a useful tool to subset primitive murine hematopoietic cells. These findings should facilitate more direct comparisons of the biology of CD34+ murine and human stem and progenitor cells.

scholarly journals EVALUATION OF INTENSITY OF HUMORAL IMMUNITY TO MEASLES AND RUBELLA IN PREGNANT WOMEN IN MOSCOW

2017 ◽  
pp. 91-98 ◽  
Author(s):  
A. V. Nozdracheva ◽  
T. A. Semenenko ◽  
S. G. Mardanly ◽  
S. V. Rotanov
Keyword(s):  
Pregnant Women ◽  
Humoral Immunity ◽  
Adult Population ◽  
Significant Proportion ◽  
Older Individuals ◽  
High Concentration ◽  
Causative Agents ◽  
Maximum Proportion ◽  
Measles Vaccination ◽  
Specific Igg

Aim. Qualitative and quantitative evaluation of humoral immunity regarding causative agents of controllable infections in pregnant women in Moscow. Materials and methods. Sera of 559 pregnant and 201 non-pregnant women were studied for the presence of antibodies against measles and rubella virus by ELISA. Results. A significant proportion of individuals seronegative to measles was detected among pregnant (21.5%) and non-pregnant (29.1%) women aged 18 - 45, that exceeds the level acceptable by regulatory requirements by 3.1 and 4.2 times, respectively. The parameter increased with age and among seropositive individuals a high concentration of IgG against measles was noted. This gives evidence, that older individuals are not covered by measles vaccination enough, and a significant part of them has post-infection immunity that is higher and more robust compared with post-vaccination. Regarding rubella infection, a more favorable situation was established: proportion of seronegative individuals among the examined was 8.9 and 10.5%, respectively. The proportion of seronegative individuals decreased with age, and by age 36 - 45 reached the minimal 4,7%. A maximum amount of rubella seronegative individuals was detected in the 26-30 age group - 12.5%, as well as maximum proportion of individuals who have high concentration of specific IgG. An increase of the amount of seronegative results was observed with the increase of gestation period for both infections. Correlation between intensity of immunity against measles and rubella in the examined women was not present. Conclusion. Means for development of extra vaccination of the adult population and execution of laboratory examination of pregnant and women planning pregnancy are proposed regarding not only rubella, but also measles.

scholarly journals High concentration tangential flow ultrafiltration of stable monoclonal antibody solutions with low viscosities

2016 ◽  
Vol 508 ◽  
pp. 113-126 ◽  
Author(s):  
Jessica J. Hung ◽  
Ameya U. Borwankar ◽  
Barton J. Dear ◽  
Thomas M. Truskett ◽  
Keith P. Johnston
Keyword(s):  
Monoclonal Antibody ◽  
High Concentration ◽  
Tangential Flow

Lyophilization Cycle Development for a High-Concentration Monoclonal Antibody Formulation Lacking a Crystalline Bulking Agent

2007 ◽  
Vol 96 (6) ◽  
pp. 1598-1608 ◽  
Author(s):  
James D. Colandene ◽  
Linda M. Maldonado ◽  
Alma T. Creagh ◽  
John S. Vrettos ◽  
Kenneth G. Goad ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Bulking Agent ◽  
High Concentration

scholarly journals Proteoglycans of hyaline cartilage: Electron-microscopic studies on isolated molecules

1975 ◽  
Vol 151 (1) ◽  
pp. 157-166 ◽  
Author(s):  
J Thyberg ◽  
S Lohmander ◽  
D Heinegård
Keyword(s):  
Hyaline Cartilage ◽  
Chondroitin Sulphate ◽  
Costal Cartilage ◽  
Side Chain ◽  
Gel Chromatography ◽  
Electron Microscopic ◽  
The Core ◽  
Central Filament ◽  
Microscopic Studies ◽  
Chondroitin Sulphate Chain

Proteoglycan monomers from guinea-pig costal cartilage, bovine nasal and bovine tracheal cartilage were observed in the electron microscope after being spread in a monomolecular layer with cytochrome c. The proteoglycan molecule appeared as an extended central core filament to which side-chain filaments were attached at various intervals. The molecules from the three sources displayed great ultrastructural similarities. On average, the core filament was about 290 nm long, there were about 25 side-chain filaments per core filament, the side-chain filaments were about 45 nm long, and the distance between the attachment points of the side-chain filaments to the core filament was about 11 nm. With regard to the overall size of the molecules, no evidence of distinct subpopulations was obtained. Good correlation was found between ultrastructural data for the proteoglycan molecules and chemical data obtained by enzyme digestions and gel chromatography. Together these data strongly support the interpretation of the electron-microscopic pictures as indicating a central filament corresponding to the protein core and side-chain filaments corresponding to the chondroitin sulphate chain clusters of the proteoglycan monomers.

Staphylococcal α-toxin: A structure-function study using a monoclonal antibody

Toxicon ◽  
1986 ◽  
Vol 24 (4) ◽  
pp. 403-411 ◽  
Author(s):  
Sidney Harshman ◽  
Nancy Sugg ◽  
Bahiru Gametchu ◽  
Robert W. Harrison
Keyword(s):  
Monoclonal Antibody ◽  
Structure Function ◽  
Toxin A ◽  
Function Study

scholarly journals Development of a mouse monoclonal antibody against the chondroitin sulfate-protein linkage region derived from shark cartilage

2010 ◽  
Vol 27 (4) ◽  
pp. 387-399 ◽  
Author(s):  
Chizuru Akatsu ◽  
Duriya Fongmoon ◽  
Shuji Mizumoto ◽  
Jean-Claude Jacquinet ◽  
Prachya Kongtawelert ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Chondroitin Sulfate ◽  
Mouse Monoclonal Antibody ◽  
Linkage Region ◽  
Shark Cartilage
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