scholarly journals Purification and Characterization of Plantaricin YKX and Assessment of Its Inhibitory Activity Against Alicyclobacillus spp.

2021 ◽  
Vol 12 ◽  
Author(s):  
Jinjin Pei ◽  
Wengang Jin ◽  
Jinze Wang ◽  
Yigang Huang ◽  
Xinsheng Li ◽  
...  
Keyword(s):  
Pore Formation ◽  
Cell Membrane Permeability ◽  
Ion Leakage ◽  
Food Label ◽  
Purification And Characterization ◽  
Minimal Inhibitory Concentrations ◽  
Flow Cytometry Data ◽  
Amino Acid Peptide ◽  
Natural Preservatives

Consumers prefer natural over synthetic chemical preservatives on a food label. Therefore, it is crucial to ensure the safety and efficacy of such natural preservatives. The emergence of heat-resistant spore-forming Alicyclobacillus spp. has been associated with spoilage problems in the fruit juice industry. Herein, a bacteriocin-producing stain YKX was isolated from the traditional pickles in Hanzhong City, China, and it was identified as Lactobacillus plantarum by morphological, biochemical, physiological, and genotypic features. A stable bacteriocin, plantaricin YKX, was isolated, purified, and tested for its efficacy against Alicyclobacillus acidoterrestris. Plantaricin YKX is a 14-amino acid peptide (Lys-Tyr-Gly-Asn-Gly-Leu-Ser-Arg-Ile-Phe-Ser-Ala-Leu-Lys). Its minimal inhibitory concentrations (MICs) against the tested bacterial and fungal strains were ranged from 16 to 64 μg/mL. It is thermostable and active at pH 3–8. The flow cytometry data and microscopic observations suggested that plantaricin YKX can augment cell membrane permeability, induce potassium ion leakage and pore formation, and disrupt cell membranes. It also affects spore germination and guaiacol production of A. acidoterrestris, probably due to upregulation of the luxS gene linked to quorum sensing.

Purification and characterization of phosphoglucomutase from peas

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger
Keyword(s):  
Purification And Characterization

Purification and Characterization of Tissue-Type Plasminogen Activator in Maxillary Mucosa with Chronic Inflammation

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi
Keyword(s):  
Plasminogen Activator ◽  
Chronic Inflammation ◽  
Gel Filtration ◽  
Potassium Acetate ◽  
Tissue Type ◽  
Purification And Characterization ◽  
Tissue Type Plasminogen Activator ◽  
Urokinase Inhibitor ◽  
Type Plasminogen Activator

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

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