Determination of the molecular weights of alginates by agarose gel filtration

1989 ◽  
Vol 465 (3) ◽  
pp. 386-389 ◽  
Author(s):  
Michio Fujihara ◽  
Terukazu Nagumo
Keyword(s):  
Gel Filtration ◽  
Agarose Gel ◽  
Molecular Weights

scholarly journals Separation and purification of the alkaline phosphatase and a phosphodiesterase from Halobacterium cutirubrum

1979 ◽  
Vol 181 (2) ◽  
pp. 347-353 ◽  
Author(s):  
P S Fitt ◽  
P Baddoo
Keyword(s):  
Alkaline Phosphatase ◽  
Gel Filtration ◽  
Adsorption Chromatography ◽  
Agarose Gel ◽  
Good Recovery ◽  
Separation And Purification ◽  
Phosphodiesterase Activity ◽  
No Adsorption ◽  
Molecular Weights ◽  
Crude Extracts

1. Halobacterium cutirubrum alkaline phosphatase is associated in crude extracts with a phosphodiesterase. 2. The enzymes were stabilized in buffers containing both (NH4)2SO4 and 10 mM-Mn2+. 3. Adsorption chromatography on Sepharose 6B/agarose-gel columns in the presence of 1.4M-(NH4)2SO4 gave a phosphatase-free phosphodiesterase and the alkaline phosphatase associated with some phosphodiesterase activity. 4. Further chromatography of the separated enzymes gave a good recovery of greater than 600-fold purified phosphodiesterase and greater than 3000-fold purified alkaline phosphatase. 5. The requirements of these enzymes and their relationship to each other was examined. 6. A detailed study showed that the alkaline phosphatase was adsorbed at least partially to agarose and dextran columns at all (NH4)2SO4 concentrations from 0.25 to 2M. 7. In contrast, no adsorption of the enzyme or protein standards was evident in 2.5M-KCl/l M-NaCl or 0.25 M-KCl/0.1 M-NaCl, in agreement with previous studies by Louis, Peterkin & Fitt [(1971) Biochem. J. 121, 635-641], thus confirming the validity of gel filtration in 2.5 M-KCl/1 M-NaCl as a method for determining the approximate molecular weights of extremehalophile proteins.

scholarly journals A Study of the Asphctic Newborn Related to Hypercoagulability by Determination of Soluble Fibrin Monomer Complex (SFMC) and Plasmin Inhibitor

1977 ◽  
Author(s):  
S. Susuki ◽  
H. Graeff ◽  
R. Hafter
Keyword(s):  
Partial Thromboplastin Time ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Newborn Infants ◽  
Agarose Gel ◽  
Significant Difference ◽  
Plasmin Inhibitors ◽  
Plasmin Inhibitor ◽  
Fibrinogen Content

Gordblood samples from 80 healthy newborns and 19 asphyctic newborns were examined. SFMG and fibrinogen were precipitated from plasma with β-alanine.Agarose gel filtration of redissolved precipitate resulted in separation of SFMC and fibrinogen. Other parameters such as TEG, Prothrombin time (PT), Partial thromboplastin time (PTT), and Plasmin-inhibitors (α2-macrogloblin, α1-antitrypsin, antithrombin III)were also determined. (Results)(1) The percent amount of SFMC of total fibrinogen content in asphyctic newborn increased 4.73 ± 1.55%, while the remaining normal infants showed only 3.17 ± 0.55% (P < 0.05)(2) In neither PT nor PTT can a significant difference be seen, although asphyctic newborn showed the tendency of hypercoagulability in TEG.(3) α1-antitrypsin (92.8 ± 21.5)and antithrombin III(8.4 ± 2.3) levels were much lower in the group with asphyxia.These results indicate that a low level of Plasmin-inhibitors act synergestically with a high activator value.The low antithrombin III level in particular could be one of the reason for the development Hypercoagulability and DIC in asphyctic newborn infants.

Bovine hepatic carboxylesterases chromatographic fractionation, gel filtration, and molecular weight estimation

1969 ◽  
Vol 47 (8) ◽  
pp. 799-805 ◽  
Author(s):  
D. J. Ecobichon
Keyword(s):  
Molecular Weight ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Bovine Liver ◽  
Weight Estimation ◽  
Molecular Weights ◽  
Starch Gel ◽  
Two Peaks ◽  
Second Peak

The carboxylesterase activity of bovine liver was fractionated by DEAE-cellulose chromatography into two peaks of activity. Electrophoresis in starch gel showed that the peak eluted first was composed of a group of five electrophoretically slow bands while the second peak was a single, rapidly migrating band. Gel filtration of the crude extract on Sephadex G-100 and G-200 yielded a single peak of esterase activity containing both the electrophoretically slow and fast bands. The determination of molecular weights by gel filtration on Sephadex G-200 and G-100 yielded estimates of 52 000 and 55 000, respectively. The molecular weight estimates of the DEAE-cellulose fractionated electrophoretically slow and fast bands on Sephadex G-100 were identical, namely 55 000.

Sign in / Sign up

Export Citation Format

Share Document