1995
DOI: 10.1002/pro.5560040922
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High-affinity binding of two molecules of cysteine proteinases to low-molecular-weight kininogen

Abstract: Human low-molecular-weight kininogen (LK) was shown by fluorescence titration to bind two molecules of cathepsins L and S and papain with high affinity. By contrast, binding of a second molecule of cathepsin H was much weaker. The 2: 1 binding stoichiometry was confirmed by titration monitored by loss of enzyme activity and by sedimentation velocity experiments. The kinetics of binding of cathepsins L and S and papain showed the two proteinase binding sites to have association rate constants k,,,,, = 10.7-24.5… Show more

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Cited by 32 publications
(40 citation statements)
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“…We have recently shown that intact human LK simultaneously can bind two molecules of cysteine proteinases with high affinity [14]. In this work we demonstrate that human HK can also bind two molecules of cathepsin S, cruzipain and papain independently.…”
mentioning
confidence: 57%
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“…We have recently shown that intact human LK simultaneously can bind two molecules of cysteine proteinases with high affinity [14]. In this work we demonstrate that human HK can also bind two molecules of cathepsin S, cruzipain and papain independently.…”
mentioning
confidence: 57%
“…The concentration of HK was determined from a molar absorbance coefficient of 63 500, calculated from the amino acid sequence [8] according to the method of Pace et al [21]. Concentrations of proteinases and of chicken cystatin were determined as described previously [14].…”
Section: Methodsmentioning
confidence: 99%
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“…The minor band probably reflects a molecule of equistatin differing Multiplication of inhibitory reactive sites has also occurred in several families of serine proteinase inhibitors (28 -30). In the case of kininogen, two (D2 and D3) of three cystatin-like domains can simultaneously inhibit papain-like cysteine proteinases (31,32). The subtle differences between both domains have significant implications for protein interactions.…”
Section: Inhibitory Specificity Of Thyroglobulin Type-1 Domains 564mentioning
confidence: 99%
“…The excitation and emission bandwidths were 5 and 10 nm, respectively. Titration of cathepsin C with chicken cystatin was performed as described previously for other cysteine proteinase-cystatin interactions [21,22] by monitoring the decrease in fluorescence emission intensity accompanying the interaction at 330 nm, where the maximum fluorescence change was observed (see Section 3). The final concentration of cathepsin C was 11.5 nM.…”
Section: Fluorescence Measurementsmentioning
confidence: 99%