PURIFICATION, CHARACTERIZATION, AND EVALUATION OF FIBRINOLYTIC ACTIVITY OF STAPHYLOKINASE FROM LOCALLY ISOLATED STAPHYLOCOCCUS AUREUS GH38

2020 ◽  
Vol 51 (4) ◽  
pp. 1195-1203
Author(s):  
Noori & Aziz
Keyword(s):  
Staphylococcus Aureus ◽  
Sodium Chloride ◽  
Ion Exchange ◽  
Fibrinolytic Activity ◽  
Therapeutic Agent ◽  
Blood Clot ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Iron Chloride ◽  
Ammonium Sulfate Precipitation

This study was aimed to purify, characteristic, and fibrinolytic activity of staphylokinase (SAK), is an enzyme activates plasminogen to form plasmin, which digest fibrin clots that cause thrombosis clot. Staphylokinase was purified from local isolate Staphylococcus aureus GH38 by ammonium sulfate precipitation at 70% saturation followed by ion exchange chromatography (CM-Cellulose) with a purification fold 2.73, and 1.53, and recovery 72.1, and 33.11% in wash and elution steps respectively. The partially purified enzyme was high activity at 40°C with pH 7 and the enzyme retained 100% of its activity at 35°C with pH 7. The activity of an enzyme increased by its treatment with calcium and sodium chloride, while the activity affected when incubated with mercury, silver, and iron chloride. The enzyme have high effective against thrombus (blood clot), which encourage the use of enzyme in the treatment as therapeutic agent to remove clots formed in the human body.

Isolation of a spermatozoal immobilization factor from Staphylococcus aureus filtrates

2009 ◽  
Vol 55 (7) ◽  
pp. 874-878 ◽  
Author(s):  
Vijay Prabha ◽  
Tanushree Gupta ◽  
Siftjit Kaur ◽  
Navchetan Kaur ◽  
Sushila Kala ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Gel Permeation Chromatography ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Human Spermatozoa ◽  
Infertile Woman ◽  
Ammonium Sulfate Precipitation ◽  
Tail Region ◽  
Sperm Immobilization

Staphylococcus aureus isolated from the cervix of an infertile woman was found to cause complete immobilization of human spermatozoa in vitro. Only the cell culture and cell-free supernatant showed immobilization activity, indicating that the sperm immobilization factor might be released extracellularly by the organism because no activity was observed with the washed cells. Heat treatment of the supernatant at 60 °C for 10 min waived its immobilizing activity, indicating that the active component may be a protein. The bioactive molecule from the supernatant was purified to homogeneity by ammonium sulfate precipitation, gel permeation chromatography, and ion exchange chromatography. Sperm immobilization factor (SIF) was found to be an ~20 kDa protein. SIF at a concentration of 10 µg/mL was required to cause 100% immobilization of human spermatozoa after 30 min of incubation at 37 °C, whereas a concentration of 150 µg/mL caused immediate immobilization, and a concentration of 200 µg/mL resulted in instant loss of viability of human spermatozoa, observed by eosin–nigrosin staining. Scanning electron microscopy showed that the treatment of human spermatozoa with SIF caused multiple defects in the head, midpiece, neck, and tail region of human spermatozoa.

USE OF GEL FILTRATION AND ION EXCHANGE CHROMATOGRAPHY FOR PARTIAL FRACTIONATION OF A SOLUTION FROM WHEY CONTAINING SODIUM CHLORIDE, ASH AND LACTOSE

1971 ◽  
Vol 34 (5) ◽  
pp. 241-243
Author(s):  
M. A. Khorshid ◽  
I. D. Rifaat ◽  
M. H. Abd El-Salam ◽  
A. A. Hofi
Keyword(s):  
Sodium Chloride ◽  
Ion Exchange ◽  
Gel Filtration ◽  
Chloride Content ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
The Other ◽  
Double Pass ◽  
Pass System ◽  
Other Hand

Lactose and chloride are partially separated from deproteinated salted whey (D.S.W.) by gel filtration. Approximately 24.1% of chloride was removed and 8.9% lactose was recovered from 3 ml of D.S.W. with a 10 g column of Sephadex G-10. On the other hand, 77.6% of chloride was removed and 74.5% lactose was recovered from 3 ml of D.S.W. with three continuous 10 g columns of Sephadax G-10. Ion exchange chromatography removed 92.1% and 99.1% of the chloride content of D.S.W. by using a single and double pass system, respectively.

Efficiency assessment of ion-exchange chromatography as the final stage of anti-VEGF antibody purification

2021 ◽  
pp. 6-9
Author(s):  
Denis Alekseevich Mazalyov ◽  
Aleksey Vladimirovich Tsivov ◽  
Viktor Andreevich Kuvshinov ◽  
Mariya Nikolaevna Zavorueva ◽  
Aleksandr Alekseevich Smirnov ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Final Stage ◽  
Therapeutic Agent ◽  
Medical Application ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Chromatographic Purification ◽  
Antibody Purification ◽  
Efficiency Assessment ◽  
Anti Vegf

The article presents the results of chromatographic purification of the anti-VEGF antibody using the ion-exchange sorbent CaptoТМ S and considers the prospects for medical application of the antibody as a therapeutic agent for cancer treatment.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Review on the Application of Mixed-mode Chromatography for Separation of Structure Isoforms

2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa
Keyword(s):  
Ion Exchange ◽  
Mixed Mode ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Charged State ◽  
Partial Structure ◽  
Reverse Phase ◽  
Oligomer Formation ◽  
Structure Rearrangement ◽  
Disulfide Scrambling

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.

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