scholarly journals Functional analysis of the effect of monoclonal antibodies on monkey liver phenylalanine hydroxylase

1986 ◽  
Vol 235 (1) ◽  
pp. 133-138 ◽  
Author(s):  
I G Jennings ◽  
R G M Russell ◽  
W L F Armarego ◽  
R G H Cotton
Keyword(s):  
Functional Analysis ◽  
Enzyme Activity ◽  
Monoclonal Antibodies ◽  
Structural Changes ◽  
Phenylalanine Hydroxylase ◽  
Functional Characteristics ◽  
Monkey Liver

An analysis of the effect of eleven monoclonal antibodies on the functional characteristics of monkey liver phenylalanine hydroxylase is presented. These eleven antibodies have been found to react with eight distinct regions on the phenylalanine hydroxylase protein. PH1 antibody inhibits enzyme activity, is dependent on phenylalanine for its binding, and appears to be related to structural changes occurring during phenylalanine activation of the enzyme activity. PH2 and PH3 antibodies stimulate enzyme activity, their binding is inhibited by lysolecithin and this group apparently is recognizing structures involved in lysolecithin activation of the enzyme activity. PH5, PH10, PH12 and PH6 recognise sites on phenylalanine hydroxylase affected by lysolecithin activation.

scholarly journals Comparative studies of four monoclonal antibodies to phenylalanine hydroxylase exhibiting different properties with respect to substrate-dependence, species-specificity and a range of effects on enzyme activity

1981 ◽  
Vol 199 (3) ◽  
pp. 527-535 ◽  
Author(s):  
K H Choo ◽  
I G Jennings ◽  
R G H Cotton
Keyword(s):  
Enzyme Activity ◽  
Monoclonal Antibodies ◽  
Comparative Studies ◽  
Phenylalanine Hydroxylase ◽  
The Other ◽  
Preliminary Characterization ◽  
Substrate Dependence ◽  
One Step ◽  
First Time

Four monoclonal antibodies to phenylalanine hydroxylase are described. Two are inhibitory (PH alpha 1-1 and PH alpha 2-1-1 antibodies), one is stimulatory (B5-1 antibody) and one has no effect on enzyme activity (PH alpha 3-0 antibody). Their properties are compared. Two antibodies (PH alpha 1-1 and B5-1 antibodies) bind primate and rodent phenylalanine hydroxylase, whereas the other two (PH alpha 2-1-1 and PH alpha 3-0 antibodies) bind only the primate enzyme. The binding of PH alpha 1-1 antibody to phenylalanine hydroxylase is dependent on substrate phenylalanine, whereas the binding of the others is not influenced by phenylalanine. Affinity adsorbents prepared from the four antibodies purified phenylalanine hydroxylase substantially (greater than 80% purity) in one step, except for a PH alpha 3-0 antibody--Sepharose column, which behaved anomalously. Two previous publications described the isolation and preliminary characterization of B5 and PH alpha 1-1 antibodies. PH alpha 2-1-1 and PH alpha 3-0 antibodies are reported for the first time.

scholarly journals Isolation of phenylalanine hydroxylase-stimulating monoclonal antibody by rat-myeloma–rat-spleen-cell fusion

1980 ◽  
Vol 191 (2) ◽  
pp. 665-668 ◽  
Author(s):  
K H Choo ◽  
J Myer ◽  
R G H Cotton ◽  
J Camakaris ◽  
D M Danks
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Spleen Cell ◽  
Cell Fusion ◽  
Phenylalanine Hydroxylase ◽  
Interesting Property ◽  
Fusion System ◽  
Hydroxylase Activity ◽  
Monkey Liver

A monoclonal antibody directed against monkey liver phenylalanine hydroxylase was produced by using a rat-myeloma–rat-spleen-cell-fusion system. This antibody showed the interesting property of increasing mammalian phenylalanine hydroxylase activity more than 2-fold. Perhaps monoclonal antibodies with this effect on other enzyme or proteins could be developed.

An Immunoradiometric Assay for Factor VIII Related Antigen (VIIIRAg) Using Two Monoclonal Antibodies-Comparison with Polyclonal Rabbit Antibodies for Use in von Willebrand’s Disease Diagnosis

1984 ◽  
Vol 52 (03) ◽  
pp. 250-252 ◽  
Author(s):  
Y Sultan ◽  
Ph Avner ◽  
P Maisonneuve ◽  
D Arnaud ◽  
Ch Jeanneau
Keyword(s):  
Monoclonal Antibodies ◽  
Structural Changes ◽  
Polyclonal Antibodies ◽  
Disease Diagnosis ◽  
Immunoradiometric Assay ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Structural Abnormalities ◽  
Antigenic Material ◽  
Von Willebrand

SummaryTwo monoclonal antibodies raised against FVIII/von Willebrand protein were used in an immunoradiometric assay (IRMA) to measure this antigen in normal plasma and plasma of patients with different forms of von Willebrand’s disease. The first antibody, an IgG1 was used to coat polystyrene tubes, the second one, an IgG2a, iodinated and used in the second step. Both antibodies inhibit ristocetin induced platelet agglutination and react strongly with platelets, megacaryocytes and endothelial cells. The IRMA test using these antibodies showed greater sensitivity than that using rabbit polyclonal anti VIIIRAg antibodies. A good correlation between the two tests was nevertheless found when VIIIRAg was measured in the majority of patient’s plasma. However 5 patients from 3 different families showed more antigenic material in the rabbit antibody IRMA than in the monoclonal antibody IRMA. It is suggested therefore that the monoclonal antibodies identify part of the VIIIR:Ag molecule showing structural abnormalities in these vWd patients, these structural changes remaining undetected by the polyclonal antibodies.

Introduction to Mistake in Contract Law

2018 ◽  
Author(s):  
Melvin A. Eisenberg
Keyword(s):  
Functional Analysis ◽  
Functional Significance ◽  
Contract Law ◽  
Second Step ◽  
Functional Characteristics ◽  
Turn On ◽  
General Parameter

Chapter 39 concerns the effect of mistake in contract law. Traditionally, contract law has recognized four categories of mistake: misunderstanding, unilateral mistake, mutual mistake, and mistranscription. The names of these categories fail to describe contractual mistakes according to their functional characteristics, and many of the rules that govern these categories turn on elements that are of only limited functional significance, easy to manipulate, or both. The first step in developing a functional analysis of mistake is to analyze contractual mistakes on the basis of their character. The second step is to analyze the rules that should govern each type of mistake based on policy, morality, and experience. This chapter sets out the general parameter of these analyses.

scholarly journals Characterization of Functional Hepatitis C Virus Envelope Glycoproteins

2004 ◽  
Vol 78 (6) ◽  
pp. 2994-3002 ◽  
Author(s):  
Anne Op De Beeck ◽  
Cécile Voisset ◽  
Birke Bartosch ◽  
Yann Ciczora ◽  
Laurence Cocquerel ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Conformational Changes ◽  
Structural Changes ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Envelope Glycoproteins ◽  
Functional Envelope

ABSTRACT Hepatitis C virus (HCV) encodes two envelope glycoproteins, E1 and E2, that assemble as a noncovalent heterodimer which is mainly retained in the endoplasmic reticulum. Because assembly into particles and secretion from the cell lead to structural changes in viral envelope proteins, characterization of the proteins associated with the virion is necessary in order to better understand how they mature to be functional in virus entry. There is currently no efficient and reliable cell culture system to amplify HCV, and the envelope glycoproteins associated with the virion have therefore not been characterized yet. Recently, infectious pseudotype particles that are assembled by displaying unmodified HCV envelope glycoproteins on retroviral core particles have been successfully generated. Because HCV pseudotype particles contain fully functional envelope glycoproteins, these envelope proteins, or at least a fraction of them, should be in a mature conformation similar to that on the native HCV particles. In this study, we used conformation-dependent monoclonal antibodies to characterize the envelope glycoproteins associated with HCV pseudotype particles. We showed that the functional unit is a noncovalent E1E2 heterodimer containing complex or hybrid type glycans. We did not observe any evidence of maturation by a cellular endoprotease during the transport of these envelope glycoproteins through the secretory pathway. These envelope glycoproteins were recognized by a panel of conformation-dependent monoclonal antibodies as well as by CD81, a molecule involved in HCV entry. The functional envelope glycoproteins associated with HCV pseudotype particles were also shown to be sensitive to low-pH treatment. Such conformational changes are likely necessary to initiate fusion.

scholarly journals Functional Analysis of the Anti-adalimumab Response Using Patient-derived Monoclonal Antibodies

2014 ◽  
Vol 289 (50) ◽  
pp. 34482-34488 ◽  
Author(s):  
Pauline A. van Schouwenburg ◽  
Simone Kruithof ◽  
Christian Votsmeier ◽  
Karin van Schie ◽  
Margreet H. Hart ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Monoclonal Antibodies
Sign in / Sign up

Export Citation Format

Share Document