Elimination of the low-molecular weight proteinase inhibitor camostate (FOY 305) and its degradation products by the rat liver

1987 ◽  
Vol 187 (6) ◽  
pp. 401-406 ◽  
Author(s):  
K. Beckh ◽  
B. Göke ◽  
R. Müller ◽  
R. Arnold
Keyword(s):  
Molecular Weight ◽  
Rat Liver ◽  
Proteinase Inhibitor ◽  
Degradation Products ◽  
Low Molecular Weight

scholarly journals The degradation of intravenously injected chondroitin 4-sulphate in the rat

1973 ◽  
Vol 134 (4) ◽  
pp. 1009-1013 ◽  
Author(s):  
Keith M. Wood ◽  
Frederick S. Wusteman ◽  
C. Gerald Curtis
Keyword(s):  
Molecular Weight ◽  
Rat Liver ◽  
Degradation Products ◽  
Chondroitin Sulphate ◽  
Whole Body ◽  
Low Molecular Weight ◽  
Inorganic Sulphate ◽  
Liver Lysosomes ◽  
Isolated Liver

The degradation of chondroitin 4-[35S]sulphate isolated from chick-embryo cartilage was studied in the rat by experiments on free-range animals, on wholly anaesthetized animals with ureter cannulae, by perfusion of isolated liver, by whole-body radioautography and by isolation of liver lysosomes. After injection into rats 68% of the radioactivity was recovered in the urine after 24h, approximately one-half of this being in the form of low-molecular-weight material, chiefly inorganic sulphate. Cannulation experiments demonstrated that the proportion of low-molecular-weight components excreted in the urine increased with time until, after 12h, virtually all was inorganic sulphate. Whole-body radioautography identified the liver as the major site of radioisotope accumulation after injection of labelled polysaccharide. Perfusion through isolated liver indicated that this organ has the ability to metabolize the polymer with the release of low-molecular-weight products, principally inorganic sulphate. Incubation of a lysosomal fraction prepared from rat liver after injection of chondroitin 4-[35S]sulphate gave rise to degradation products of low molecular weight, and experiments in vitro with rat liver lysosomes confirmed that these organelles are capable of the entire degradative process from chondroitin sulphate to free inorganic sulphate.

Instabilities in the System NMMO/Water/Cellulose (Lyocell Process) Caused by Polonowski Type Reactions

Holzforschung ◽  
2002 ◽  
Vol 56 (2) ◽  
pp. 199-208 ◽  
Author(s):  
Thomas Rosenau ◽  
Antje Potthast ◽  
Andreas Hofinger ◽  
Herbert Sixta ◽  
Paul Kosma
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Exchange Resin ◽  
Degradation Products ◽  
Ion Exchange Resin ◽  
Low Molecular Weight ◽  
Acid Component ◽  
Degradation Reactions ◽  
Polyglucuronic Acid

Summary Polonowski type degradation reactions are a major reason for the frequently observed instability of solutions of cellulose in N-methylmorpholine-N-oxide monohydrate (NMMO, 1). The degradation is induced by degradation products of cellulose and NMMO generated in situ in the Lyocell system. The presence of both an amine component, such as morpholine or N-methylmorpholine, and an acid component is required for the decomposition process to proceed. The latter might be a low-molecular-weight compound, such as formic acid, acetic acid or gluconic acid, or also a high-molecular-weight acid, such as polyglucuronic acid or ion exchange resin.

Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor

1987 ◽  
Vol 247 (1) ◽  
pp. 187-193 ◽  
Author(s):  
U. Rausch ◽  
G. Adler ◽  
H. Weidenbach ◽  
F. Weidenbach ◽  
D. Rudolff ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Secretory Process ◽  
Low Molecular Weight ◽  
Stimulation Of

Low-molecular-weight proteinase inhibitor of human epidermis inhibiting papain and trypsin activity

1986 ◽  
Vol 278 (3) ◽  
pp. 194-198 ◽  
Author(s):  
I. Takiuchi ◽  
H. Takagi ◽  
H. Goi ◽  
M. Kawamura ◽  
D. Higuchi
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Human Epidermis ◽  
Low Molecular Weight ◽  
Trypsin Activity

BINDING AND METABOLISM OF HEPARIN BY ENDOTHELIAL CELLS

1987 ◽  
Author(s):  
S Vannucchi ◽  
F Pasquali ◽  
P Bianchi-ni ◽  
M Ruggiero
Keyword(s):  
Molecular Weight ◽  
Endothelial Cells ◽  
De Novo ◽  
Degradation Products ◽  
Low Molecular Weight ◽  
Competition Binding ◽  
Capillary Endothelial Cells ◽  
A Site ◽  
Binding Sequence

In this study we show that bovineadrenal capillary endothelial cells(BACE) contain heparin (HP); this HP has been found associated with the cell surface (i.e; trypsin-removable^and intracellularly. How-ever, experiments with [ sjsodium sulfate labelling, demonstrate that BACE cells donot synthesize HP de novo, but they uptake it from serum. We have studied binding, uptake, and metabolism odifferent molecular weight-HPs: 13 Kd-HP from bovine source, 14 Kd-HP from porcine source, 4.5 Kd, and 2.5-HP fragments. Comparison among different HPs, was carried out by calculating the IC from competition curves for [3HJ- HP. Binding of labelled-HP to BACE cells was specificand saturable. Dextran sulfate and glycosaminoglycans did not compete for binding; only heparan sulfate showed some competition. Binding of different HPs was strictly dependent on their molecular weight; 2.5 Kd- HP was unable to bind to cells, although sulfation degree of this fragment and of unfractionated HP was almost identical. Therefore, we assume that a specific oligosaccharide sequence could be responsible for HP binding to BACE cells; this hypothetical "binding sequence" could then be lost in very low molecular weight-HP fragments. BACE cells are also able to internalize HP, and they release its low molecular weight degradation products into culture medium. Thus we suggest that endothelial cells might represent a site for the metabolism of endogenous and exogenous HP in vivo.

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