Immunochemical Confirmation of the Primary Structure of Streptococcal Hyaluronan Synthase and Synthesis of High Molecular Weight Product by the Recombinant Enzyme

Biochemistry ◽  
1994 ◽  
Vol 33 (31) ◽  
pp. 9033-9039 ◽  
Author(s):  
Paul L. DeAngelis ◽  
Paul H. Weigel
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Primary Structure ◽  
Recombinant Enzyme ◽  
Hyaluronan Synthase ◽  
High Molecular Weight Product ◽  
Molecular Weight Product

Lignin-Carbohydrate Condensation Product Formation in a Biomimetic Model Pulp Bleaching System

Holzforschung ◽  
2003 ◽  
Vol 57 (4) ◽  
pp. 385-390 ◽  
Author(s):  
C. C. Walker ◽  
T. J. McDonough ◽  
R. J. Dinus ◽  
K.-E. L. Eriksson
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Condensation Product ◽  
Condensation Reaction ◽  
Product Formation ◽  
Water Soluble ◽  
Hydroxyethyl Cellulose ◽  
Pulp Bleaching ◽  
High Molecular Weight Product ◽  
Molecular Weight Product

Abstract Three biomimetic compounds were evaluated for their ability to preferentially degrade lignin in the presence of carbohydrate using two water-soluble polymeric model compounds: lignosulfonate and hydroxyethyl cellulose (HEC). The three biomimetic systems studied were FeSO4, Fe-EDTA and hemoglobin, each in the presence of hydrogen peroxide. When both polymeric substrates were present, a high molecular weight product was observed to form upon addition of H2O2. This high molecular weight product is believed to be the result of a condensation reaction between lignosulfonate and HEC. The condensation product was also observed to form in the absence of biomimetic catalyst. For all reactions, the molecular weight of the condensation product was observed to decrease with increasing reaction time. By altering the ratio of lignosulfonate to HEC, a limit was observed in the relative amount of condensation product formed. The formation of this condensation product is believed to limit the effectiveness of acidic bleaching systems.

Uptake and Catabolism of 125l-Thrombin by the Rabbit Thoracic Aorta In Vitro: Permeability of the Endothelium, Intima-Media and Adventitial Layers

1984 ◽  
Vol 52 (02) ◽  
pp. 105-111 ◽  
Author(s):  
Mark W C Hatton ◽  
Sue L Moar
Keyword(s):  
Molecular Weight ◽  
Endothelial Cells ◽  
Vessel Wall ◽  
Antithrombin Iii ◽  
High Molecular Weight Product ◽  
Constant Rate ◽  
Molecular Weight Product ◽  
Media Layer ◽  
Extracellular Proteolysis

SummaryThe uptake, distribution and catabolism of 125I-thrombin has been studied in vitro using normal and ballooned (de-endothelialized) aorta segments at 37° C and at 4° C. In addition to rapid uptake by endothelial cells, 125I-thrombin passed at a slower, and yet constant, rate through the endothelium and accumulated in the intima-medial and adventitial layers. The enzyme, however, was not able to cross the adventitia. Passage through the endothelium was probably intercellular rather than due to transcytosis. Uptake by the intima-media layer of ballooned segments was substantially faster (× 2.5) than by the subendothelial (intima-media) region of normal segments. Once associated with the endothelium and the subendothelial layers, 125I-thrombin was catabolized and radioactive products, which were released from the vessel wall, appeared in the incubation medium. Two possible catabolic routes were identified: 1. the enzyme was recovered as a high molecular weight product (i. e. excluded by Sephadex G-200), due to complex formation with an extracellular vessel wall component and/or plasma antithrombin III. 2. Fragments of the enzyme were recovered which were presumably the products of limited, extracellular proteolysis.

scholarly journals Primary structure of high molecular weight tau present in the peripheral nervous system.

1992 ◽  
Vol 89 (10) ◽  
pp. 4378-4381 ◽  
Author(s):  
D. Couchie ◽  
C. Mavilia ◽  
I. S. Georgieff ◽  
R. K. Liem ◽  
M. L. Shelanski ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Nervous System ◽  
High Molecular Weight ◽  
Peripheral Nervous System ◽  
Primary Structure

Characterization Of A Crosslink-Containing Fragment Derived From The A Polymer Of Human Fibrin And Its Application In Immunologic Studies Using Monoclonal Antibodies

1981 ◽  
Author(s):  
J H Sobel ◽  
S Birken ◽  
P Ehrlich ◽  
R Friedman ◽  
Z Moustafa ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibodies ◽  
Early Detection ◽  
High Molecular Weight ◽  
Primary Structure ◽  
Cyanogen Bromide ◽  
Tryptic Peptide ◽  
Structural Studies ◽  
Polymer Component

A high molecular weight crosslink-containing fragment derived from cyanogen bromide (CNBr) digests of the a polymer component of human fibrin has been isolated and characterized. The material has been used to generate monoclonal antibodies toward the goals of (1) producing fibrin-specific probes for use in the early detection of thrombosis and (2) generating monoclonal lines to single determinants in the COOH-terminal region of the Aα chain for use in structural studies of fibrinogen and fibrin.Biochemical and immunologic characterization data indicate the fragment is comprised, predominantly, of equimolar quantities of the CNBr peptides spanning residues #241-476 (CNBr 8) and #518-584 (CNBr 10) in the original Aα chain. The acceptor and donor units are crosslinked via an average of 2.8-3.2 ε-(γ-glutamyl) lysine bonds per mole of CNBr 8 + CNBr 10 producing heterogeneously sized fragments in the range of 80,000-200,000 daltons.Two types of monoclonal lines have been obtained. The first react with regions of primary structure and in one instance immunoreactivity could be localized to the Aa tryptic peptide #253-268. The second type appear to recognize conformational determinants as shown by one antibody that reacts well with the CNBr crosslinked fragment but poorly with its constituent peptides.

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