Identification and characterization of antibodies elicited by human cystatin C fragment

2017 ◽  
Vol 31 (4) ◽  
pp. e2689
Author(s):  
Izabela Behrendt ◽  
Martyna Prądzińska ◽  
Marta Spodzieja ◽  
Paulina Czaplewska ◽  
Aleksandra S. Kołodziejczyk ◽  
...  
Keyword(s):  
Cystatin C ◽  
Human Cystatin C ◽  
Identification And Characterization ◽  
Human Cystatin

Isolation and characterization of autoantibodies against human cystatin C

Amino Acids ◽  
2016 ◽  
Vol 48 (11) ◽  
pp. 2501-2518 ◽  
Author(s):  
Martyna Prądzińska ◽  
Izabela Behrendt ◽  
Marta Spodzieja ◽  
Aleksandra S. Kołodziejczyk ◽  
Sylwia Rodziewicz-Motowidło ◽  
...  
Keyword(s):  
Cystatin C ◽  
Isolation And Characterization ◽  
Human Cystatin C ◽  
Human Cystatin

scholarly journals Structural characterization of V57D and V57P mutants of human cystatin C, an amyloidogenic protein

2013 ◽  
Vol 69 (4) ◽  
pp. 577-586 ◽  
Author(s):  
Marta Orlikowska ◽  
Aneta Szymańska ◽  
Dominika Borek ◽  
Zbyszek Otwinowski ◽  
Piotr Skowron ◽  
...  
Keyword(s):  
Cystatin C ◽  
Structural Characterization ◽  
Human Cystatin C ◽  
Amyloidogenic Protein ◽  
Human Cystatin

scholarly journals Papain labelled with fluorescent thiol-specific reagents as a probe for characterization of interactions between cysteine proteinases and their protein inhibitors by competitive titrations

1991 ◽  
Vol 276 (2) ◽  
pp. 387-394 ◽  
Author(s):  
P Lindahl ◽  
E Raub-Segall ◽  
S T Olson ◽  
I Björk
Keyword(s):  
Cystatin C ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Equilibrium Constants ◽  
Sulphonic Acid ◽  
Cysteine Proteinases ◽  
Human Cystatin C ◽  
Human Cystatin ◽  
Chicken Cystatin

Papain was labelled by attachment of the fluorescent groups 2-(4′-acetamidoanilino)naphthalene-6-sulphonic acid (AANS) or N-(acetylaminoethyl)-8-naphthylamine-1-sulphonic acid (AEDANS) to the active-site cysteine residue, with the aim of using the labelled papains as probes in competitive titrations of unlabelled cysteine proteinases with their inhibitors. The interaction between the labelled papains and cystatins was accompanied by an increase in fluorescence emission of up to 38-fold for AANS-papain and approximately 3.5-fold for AEDANS-papain. Fluorescence titrations gave dissociation equilibrium constants of 3.1 and 0.6 microM for the binding of chicken cystatin and recombinant human cystatin C respectively to AANS-papain and of 11.9 microM for the binding of chicken cystatin to AEDANS-papain. The kinetics of interaction of chicken cystatin with AANS-papain showed an unusual biphasic dependence of the observed pseudo-first-order rate constant on inhibitor concentration, consistent with the reaction occurring via both pathways of a general two-step binding mechanism. AANS-papain was selected as the most suitable probe for competitive titrations of unlabelled active or inactivated cysteine proteinases with inhibitors. This technique, which provides stoichiometries and dissociation constants for the interaction between unlabelled enzyme and inhibitor, allows monitoring of the interactions by a large fluorescent signal in a wavelength region where the interacting proteins do not contribute to the observed fluorescence. Such competitive titrations of active papain or actinidin with chicken cystatin or recombinant human cystatin C all gave inhibitor/enzyme stoichiometries of close to 1.0. A dissociation constant of 1.8 microM for the reaction of chicken cystatin with a papain derivative, S-[N-(3-carboxypropyl)succinimidyl]-papain, was also determined by the same technique. These results show the usefulness of the fluorescent papains for the characterization of interactions between cysteine-proteinase inhibitors and their target enzymes.

Affinity Purification and Elimination of Methionine Oxidation in Recombinant Human Cystatin C

1997 ◽  
Vol 11 (1) ◽  
pp. 111-118 ◽  
Author(s):  
Paul J. Berti ◽  
Irena Ekiel ◽  
Peter Lindahl ◽  
Magnus Abrahamson ◽  
Andrew C. Storer
Keyword(s):  
Cystatin C ◽  
Affinity Purification ◽  
Methionine Oxidation ◽  
Human Cystatin C ◽  
Human Cystatin

scholarly journals Application of amide hydrogen/deuterium exchange mass spectrometry for epitope mapping in human cystatin C

Amino Acids ◽  
2016 ◽  
Vol 48 (12) ◽  
pp. 2809-2820 ◽  
Author(s):  
Martyna Prądzińska ◽  
Izabela Behrendt ◽  
Juan Astorga-Wells ◽  
Aleksandr Manoilov ◽  
Roman A. Zubarev ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cystatin C ◽  
Epitope Mapping ◽  
Hydrogen Deuterium Exchange ◽  
Amide Hydrogen ◽  
Exchange Mass Spectrometry ◽  
Human Cystatin C ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry ◽  
Human Cystatin
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