Osmotic coefficients of urea + guanidinium chloride mixtures in water at 298.15 K

1982 ◽  
Vol 78 (7) ◽  
pp. 2275 ◽  
Author(s):  
Terence H. Lilley ◽  
Dennis R. Tester
Keyword(s):  
Osmotic Coefficients ◽  
Guanidinium Chloride

Inactivation Kinetics of β-N-Acetyl-D-glucosaminidase from Green Crab (Scylla serrata) by Guanidinium Chloride

2012 ◽  
Vol 19 (11) ◽  
pp. 1177-1182
Author(s):  
Ji-Ping Zhang ◽  
Bo Leng ◽  
Qian-Sheng Huang ◽  
Ya-Wen Yan ◽  
Xuan Liu ◽  
...  
Keyword(s):  
Green Crab ◽  
Scylla Serrata ◽  
Inactivation Kinetics ◽  
Guanidinium Chloride ◽  
Kinetics Of

scholarly journals Isolation of human synovial-fluid hyaluronate by density-gradient ultracentrifugation and evaluation of its protein content

1972 ◽  
Vol 126 (5) ◽  
pp. 1073-1080 ◽  
Author(s):  
Irwin Scher ◽  
David Hamerman
Keyword(s):  
Synovial Fluid ◽  
Density Gradient ◽  
Density Gradient Ultracentrifugation ◽  
Proteolytic Digestion ◽  
Peptide Fragments ◽  
Guanidinium Chloride ◽  
Caesium Chloride ◽  
Normal Human ◽  
Protein Moiety ◽  
Human Synovial Fluid

1. A compound of hyaluronate and protein, called hyaluronate–protein was isolated from pooled human synovial fluids by caesium chloride density-gradient ultracentrifugation. 2. The isolated hyaluronate–protein was labelled with [125I]iodide and the following studies were done. (a) Ultracentrifugation in caesium chloride showed that the protein moiety (125I counts) and hyaluronate (hexuronate) sedimented together in the middle of the gradient. (b) The labelled hyaluronate–protein was treated with trypsin, and ultracentrifugation showed that peptide fragments (125I counts) were dispersed throughout the gradient, indicating proteolytic digestion. Hyaluronate sedimented in the middle of the gradient. (c) The labelled hyaluronate–protein was digested with streptococcal hyaluronidase, and ultracentrifugation showed that hyaluronate fragments were dispersed throughout the gradient, indicating digestion of the polysaccharide. The protein moiety, without attached hyaluronate, now sedimented at the top of the gradient. (d) Ultracentrifugation of labelled hyaluronate–protein in 4m-guanidinium chloride showed that protein and hyaluronate sedimented together. 3. These studies confirm that hyaluronate is combined with a small quantity of protein in normal human synovial fluid. A mild method for the rapid isolation of hyaluronate–protein in good yield is described.

ChemInform Abstract: Isopiestic Determination of Osmotic Coefficients at 100 °C by Means of a Simple Apparatus

ChemInform ◽  
1989 ◽  
Vol 20 (6) ◽  
Author(s):  
K. GRJOTHEIM ◽  
W. VOIGT ◽  
B. HAUGSDAL ◽  
D. DITTRICH
Keyword(s):  
Osmotic Coefficients ◽  
Simple Apparatus

scholarly journals Metabolism of rat bone proteoglycans in vivo

1983 ◽  
Vol 216 (3) ◽  
pp. 589-596 ◽  
Author(s):  
C W Prince ◽  
F Rahemtulla ◽  
W T Butler
Keyword(s):  
Extraction Procedure ◽  
Total Radioactivity ◽  
Mineralized Tissue ◽  
Guanidinium Chloride ◽  
Disaccharide Composition ◽  
A Minor ◽  
Papain Digestion ◽  
Rat Bone

Former evaluations of the role of proteoglycans in mineralization have neglected to address the possibility that the metabolism of proteoglycans may be of significance in this regard. This problem was studied by using radiolabeling in vivo of rat calvaria with [35Sulphate for 2-72 h and a sequential extraction procedure to yield two pools of newly synthesized proteoglycans: one obtained from non-mineralized tissue by extraction with guanidinium chloride (GdmCl) and another obtained only after demineralization with EDTA. Total radioactivity in calvaria was maximal after 12 h of incorporation, but by 36 h had declined to a level that was about 55-65% of maximum. Radioactivity in the GdmCl extract declined steadily after 12 h, whereas that in the EDTA extract remained constant until 36 h, when it began to increase. Each extract contained a minor proteoglycan that eluted at the void volume (Vo) of a Sepharose CL-6B column. Unlike in the EDTA extract, this proteoglycan gradually disappeared from the GdmCl extract. Each extract also contained a major, smaller proteoglycan, with a Kav. of 0.24 and 0.36 in the GdmCl and EDTA extracts respectively. Papain digestion of each extract yielded glycosaminoglycan chains with Kav. values of 0.32 and 0.50 on CL-6B in the GdmCl and EDTA extracts respectively. Digestion of each extract with chondroitinase ABC and chondroitinase AC showed that the glycosaminoglycans were of similar disaccharide composition, with about 85% being 4-sulphated and the remainder 6-sulphated and/or iduronic acid-containing. These data suggest that about 45% of the newly synthesized proteoglycans are removed from the tissue during the course of mineralization.

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