Specific Affinity Labeling ofμOpioid Receptors by S-Activated Enkephalin Analog Containingp-Nitrophenylalanine

1994 ◽  
Vol 67 (1) ◽  
pp. 296-299 ◽  
Author(s):  
Teruo Yasunaga ◽  
Yasuyuki Shimohigashi ◽  
Hiroaki Kodama ◽  
Masaya Miyazaki ◽  
Masaya Nagaishi ◽  
...  
Keyword(s):  
Affinity Labeling ◽  
Specific Affinity

Specific affinity labeling of μ opioid receptors in rat brain by S-activated sulfhydryldihydromorphine analogs

1995 ◽  
Vol 5 (15) ◽  
pp. 1609-1614 ◽  
Author(s):  
Takeshi Sagara ◽  
Mikako Okamura ◽  
Yasuyuki Shimohigashi ◽  
Motonori Ohno ◽  
Ken Kanematsu
Keyword(s):  
Rat Brain ◽  
Opioid Receptors ◽  
Affinity Labeling ◽  
Specific Affinity ◽  
Μ Opioid Receptors

Specific affinity-labeling of the nociceptin ORL1 receptor using a thiol-activated Cys(Npys)-containing peptide ligand

Biopolymers ◽  
2016 ◽  
Vol 106 (4) ◽  
pp. 460-469 ◽  
Author(s):  
Ayami Matsushima ◽  
Hirokazu Nishimura ◽  
Yutaka Matsuyama ◽  
Xiaohui Liu ◽  
Tommaso Costa ◽  
...  
Keyword(s):  
Affinity Labeling ◽  
Peptide Ligand ◽  
Orl1 Receptor ◽  
Specific Affinity

m-[o-(2-Chloro-5-Fluorosulfonylphenylureido)Phenoxybutoxy]Benzamidine: Affinity Labeling Reagent Which Can Identify Secondary Binding Sites of Coagulation Complement and Fibrinolytic Serine Proteases

1979 ◽  
Author(s):  
D Bing ◽  
D Robison ◽  
J Andrews ◽  
R Laura
Keyword(s):  
Binding Sites ◽  
Serine Proteases ◽  
Enzyme Inhibitor ◽  
Molecular Model ◽  
Factor Xa ◽  
Affinity Labeling ◽  
Catalytic Center ◽  
Inhibitor Complex ◽  
Polypeptide Chains ◽  
Kinetics Of

We have determined that m-[o-(2-chloro-5-fluorosulfonylphenylureido)phenoxybutoxy]benza-midine [mCP(PBA)-F] is an affinity labeling reagent which labels both polypeptide chains of thrombin, factor Xa, complement component CIS and plasmin. As this means it is reacting outside of the catalytic center, we have called this reagent an exo-site affinity labeling reagent. Progressive irreversible inhibition of these enzymes by this reagent is rapid (k1st 2.5-4.6 x 10-3sec-1), the kinetics of inactivation are consistent with inhibition proceding via formation of a specific enzyme-inhibitor complex analogous to a Michaelis-Menton complex (KL - 115-26 μM), and diisopropylfluorophosphate or p-amidino-phenylmethanesulfonyfluoride Prevent labeling by [3H]mCP(PBA)-F. A molecular model of mCP(PBA)-F shows that the reactive SO2F group can be 17 A from the cationic amidine. The data are consistent with the hypothesis that both peptide chains are required for the specific proteolytic activity exhibited by these proteases and that the peptide chain which does not contain the active site serine is close to the catalytic center. (Supported by NIH and AHA grants

scholarly journals Possibility of Japanese Cedar Pollen Causing False Positives in the Deep Mycosis Test

2021 ◽  
Vol 22 (4) ◽  
pp. 2135
Author(s):  
Takashi Kanno ◽  
Changmin Kim ◽  
Daisuke Yamanaka ◽  
Ken-ichi Ishibashi ◽  
Hiroshi Tanaka ◽  
...  
Keyword(s):  
Quantitative Methods ◽  
Japanese Cedar ◽  
False Positives ◽  
Affinity Column ◽  
Deep Mycosis ◽  
Specific Affinity ◽  
Japanese Cedar Pollen ◽  
Cedar Pollen ◽  
Positive Factor ◽  
Lal Assay

Because Japanese cedar pollen (JCP) contains beta-1,3-d-glucan (BG), there is concern that its lingering presence in the atmosphere, especially during its scattering period, may cause false positives in the factor-G-based Limulus amebocyte lysate (LAL) assay used to test for deep mycosis (i.e., G-test). Hence, we examined whether the LAL assay would react positively with substances contained in JCP by using the G-test to measure JCP particles and extracts. BG was purified from the JCP extract on a BG-specific affinity column, and the percentage extractability was measured using three different BG-specific quantitative methods. The G-test detected 0.4 pg BG in a single JCP particle and 10 fg from a single particle in the extract. The percentage extractability of JCP-derived BG was not significantly different among the three quantitative methods. As the JCP particles should technically have been removed during serum separation, they should be less likely to be a direct false-positive factor. However, given that the LAL-assay-positive substances in the JCP extract were not distinguishable by the three BG-specific quantitative methods, we conclude that they may cause the background to rise. Therefore, in Japan false positives arising from JCP contamination should be considered when testing patients for deep mycosis.

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