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Article | 16-October-2019

Cold autoadsorption

Ernest M. Ekema

Immunohematology, Volume 34 , ISSUE 4, 158–160

Article | 14-October-2020

Low-incidence MNS antigens associated with single amino acid changes and their susceptibility to enzyme treatment

identified changes in amino acids that are associated with several low-incidence antigens in the MNS blood group system. This review relates the molecular studies with the susceptibility or resistance of these antigens to treatment of intact red blood cells by proteolytic enzymes.

Marion E. Reid, Jill Storry

Immunohematology, Volume 17 , ISSUE 3, 76–81

Original Paper | 04-December-2017

Characterization of Bacteriocin-Producing Lactic Acid Bacteria Isolated from Native Fruits of Ecuadorian Amazon

method the active synthetized components released in the neu­tralized and hydroxide peroxide eliminated cell-free supernatant were inhibited by proteolytic enzymes, while the activity was maintained stable after the treatment with catalase, lysozyme, α-amylase and lipase suggesting their proteinaceous nature. The inhibitory activity was stimulated by acidic conditions, upon exposure to high heat and maintained stable at different ranges of sodium chloride (4–10%). The DNA sequencing

Karina Garzón, Clara Ortega, Gabriela N. Tenea

Polish Journal of Microbiology, Volume 66 , ISSUE 4, 473–481

Article | 17-November-2020

Application of the proteolytic enzyme papain in routine platelet serology

The use of proteolytic enzymes is well established in red cell serology. These enzymes modify some antigen structures and remove sialic acid from the red cell membrane. Enzyme-sensitive structures have also been identified on the platelet membrane. The effect of papain, a proteolytic enzyme used widely in red cell serology, on the detection of various platelet alloantibodies was examined to determine its usefulness in platelet serology. Antisera with the specificities anti-HPA-la, -2b, -3a, -4a

John A.G. Lown, Brian J. Dale

Immunohematology, Volume 11 , ISSUE 4, 140–142

Research Article | 22-May-2019

CHARACTERISTICS AND POTENTIAL APPLICATIONS OF CIRCULAR BACTERIOCINS

Bacteriocins are ribosomally synthesized peptides or proteins exerting anatagonistic activity toward organisms which are closely related to the producer strain. Circular bacteriocins are produced by Gram-positive bacteria, mainly lactic acid bacteria, and to a lesser extent by Bacillus, Clostridium and Staphylococcus genera. These bacteriocins are characterized by the head-to-tail cyclization of their backbone. The circular nature of these peptides makes them resistant to many proteolytic

Urszula Błaszczyk, Kamila Dąbrowska

Postępy Mikrobiologii - Advancements of Microbiology, Volume 56 , ISSUE 4, 451–464

Original Paper | 30-June-2018

Isolation of Bacteriocin-producing Staphylococcus spp. Strains from Human Skin Wounds, Soft Tissue Infections and Bovine Mastitis

isolated from the infected human skin wound. Three of the six antimicrobials produced by the different strains showed substantial loss of antimicrobial activity upon treatment with proteolytic enzymes, which suggests their peptidic structure. Additional studies have shown that one of the putative bacteriocins was efficiently secreted to the liquid medium, facilitating its large-scale production and isolation. The peptide produced by the M2B strain exhibited promising activity; however, against narrow

MAGDALENA ZALEWSKA, JOHN J. CHUREY, RANDY W. WOROBO, SŁAWOMIR MILEWSKI, PIOTR SZWEDA

Polish Journal of Microbiology, Volume 67 , ISSUE 2, –

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