Heat Denaturation and Emulsifying Properties of Plasma Protein

1987 ◽  
Vol 51 (10) ◽  
pp. 2787-2792
Author(s):  
Masayoshi Saito ◽  
Harue Taira
1990 ◽  
Vol 37 (10) ◽  
pp. 805-809 ◽  
Author(s):  
Masayoshi SAITO ◽  
Emiko ISHIBASHI ◽  
Harue TAIRA

1977 ◽  
Vol 16 (03) ◽  
pp. 100-103 ◽  
Author(s):  
C. Schümichen ◽  
J. Waiden ◽  
G. Hoffmann

SummaryThe kinetic data of two different 99mTc-Sn-pyrophosphate compounds (compound A and B) were evaluated in non-adult rats. Only compound A concentrated in bone. Both compounds dispersed rapidly in the intravascular as well as the extravascular space. The plasma protein bond of both compounds increased with time after injection and impaired both the renal clearance of both compounds and the bone clearance of compound A. The renal clearance of both compounds was somewhat above that of 5 1Cr-EDTA. It is concluded that compound A and B is mainly excreted by glomerular filtration. About one fourth of the glomerular filtrate of compound B is reabsorbed and accumulated by the tubular cells.


1974 ◽  
Vol 31 (03) ◽  
pp. 395-402 ◽  
Author(s):  
V Bocci ◽  
T Conti ◽  
M Muscettola ◽  
A Pacini ◽  
G. P Pessina

SummaryRabbit fibrinogen digest products (FDP) have been separated by Pevikon block electrophoresis yielding fragments D, E and other unidentified FDP.The fragments were injected into rabbits. Surprisingly, as little as 4.3 mg of fragment D elicited a significant increase in plasma fibrinogen concentration 24 hr after injection. The stimulating activity of fragment D is at least 10-fold higher than that of fragment E.


1964 ◽  
Vol 11 (01) ◽  
pp. 064-074 ◽  
Author(s):  
Robert H Wagner ◽  
William D McLester ◽  
Marion Smith ◽  
K. M Brinkhous

Summary1. The use of several amino acids, glycine, alpha-aminobutyric acid, alanine, beta-alanine, and gamma-aminobutyric acid, as plasma protein precipitants is described.2. A specific procedure is detailed for the preparation of canine antihemophilic factor (AHF, Factor VIII) in which glycine, beta-alanine, and gammaaminobutyric acid serve as the protein precipitants.3. Preliminary results are reported for the precipitation of bovine and human AHF with amino acids.


1985 ◽  
Vol 53 (01) ◽  
pp. 005-007 ◽  
Author(s):  
I Pabinger-Fasching ◽  
K Lechner ◽  
H Niessner ◽  
P Schmidt ◽  
E Balzar ◽  
...  

SummaryIn patients with severe nephrotic syndrome determinations of plasma protein C : Ag levels (8 patients: 5 adults, 3 children) and protein C activity (3 out of 8 patients) revealed significantly elevated plasma protein C concentrations. Furthermore we observed a significant inverse correlation of protein C : Ag to AT III : Ag levels. No protein C : Ag could be detected in the urine of two patients studied. We conclude from our data, that changes of plasma protein C do not contribute to the high thrombotic tendency in nephrotic syndrome.


2014 ◽  
Vol 11 (1) ◽  
pp. 29
Author(s):  
Nonnah Ismail ◽  
Juliana Mahmod ◽  
Awatif Khairul Fatihin Mustafa Kamal

In this study, Hydrolysate from angelwing clam (Pholas orientalis) was produced at 0, 1, 2 and 3 hrs and E/S ratio of0.5 and 3%using alcalase where the pH and temperature were kept constant at pH 8.5 and 60°C, respectively. The hydrolysates were analysed for antioxidant and functional properties such as solubility, emulsifying properties and water and oil holding capacity. Degree of hydrolysis (DH), yield, functional and antioxidant properties were influenced by the hydrolysis time and E/S ratio. Higher enzyme concentration (E/S 3%) and longer hydrolysis time increased the DH. Yield was higher at E/S 3% but reduced with hydrolysis time. Longer hydrolysis time produced more soluble hydrolysate and higher metal chelating activity but lower in emulsifying properties and DPPH activity. Higher enzyme concentration resulted in increase only in solubility and metal chelating activity. This study revealed that enzymatic hydrolysis using alcalase should be performed at shorter hydrolysis time using intermediate concentration of enzyme (E/S between 0.5 to 3%) in order to produce angelwing clam hydrolysate with collectively good functional and antioxidant properties. 


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