Binding of α2-macroglobulin and haptoglobin to Actinomyces pyogenes

1985 ◽  
Vol 31 (7) ◽  
pp. 657-659 ◽  
Author(s):  
Christoph Lämmler ◽  
Gursharan S. Chhatwal ◽  
Hans Blobel
Keyword(s):  
Immunoglobulin G ◽  
Steric Hindrance ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Binding Activity ◽  
The Other ◽  
Α2 Macroglobulin ◽  
Protein Nature ◽  
Actinomyces Pyogenes

All 25 cultures of Actinomyces pyogenes tested in the present study bound 125I-labelled human α2-macroglobulin with a mean binding of 65.6%. Thirteen cultures also bound 125I-labelled human haptoglobin with a mean of 51.5%. None interacted with fibrinogen, fibronectin, immunoglobulin G, or albumin. Twenty-eight cultures representing other species of actinomycetaceae did not show any interaction with α2-macroglobulin, haptoglobin, and other plasma proteins tested. The binding of α2-macroglobulin and haptoglobin to A. pyogenes was saturable and could be completely inhibited by the respective unlabelled plasma proteins. The binding of α2-macroglobulin could not be inhibited by unlabelled haptoglobin. On the other hand, α2-macroglóbulin blocked the binding of haptoglobin, possibly by steric hindrance. Treatment of the bacteria with trypsin reduced their binding activities for α2-macroglobulin and haptoglobin indicating the protein nature of the binding sites. Exposure to heat (1 h, 80 °C) significantly diminished the binding activity for haptoglobin, but not that for α2-macroglobulin. The binding of α2-macroglobulin and haptoglobin could be an important feature in the classification of A. pyogenes among the members of actinomycetaceae.

MONOCLONAL ANTIBODIES THAT RECOGNIZE Ca2+-INDUCED CONFORMER OF PROTEIN C, INDEPENDENT OF GLA RESIDUES

1987 ◽  
Author(s):  
T Sugo ◽  
S Tanabe ◽  
K Shinoda ◽  
M Matsuda
Keyword(s):  
Monoclonal Antibodies ◽  
Light Chain ◽  
Metal Binding ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Protein C ◽  
The Other ◽  
Metal Binding Sites ◽  
Direct Elisa ◽  
Gla Domain

Monoclonal antibodies (MCA’s) were prepared against human protein C (PC) according to Köhler & Milstein, and those that recognize the Ca2+-dependent PC conformers were screened by direct ELISA in the presence of 2 mM either CaCl2 or EDTA. Out of nine MCAߣs thus screened, five MCA's designated as HPC-1˜5, respectively, were found to react with PC in the presence of Ca2+ but not EDTA. By SDS-PAGE coupled with Western Blotting performed in the presence of 2 mM CaCl2, we found that two MCA’s HPC-1 and 2, recognized the light chain, and two others, HPC-3 and 4, recognized the heavy chain of PC. But another MCA, HPC-5 was found to react with only non-reduced antigens. Further study showed that HPC-1 and 5 failed to react with the Gla-domainless PC, i.e. PC from which the N-terminal Gla-domain of the light chain had been cleaved off by α-chymotrypsin. However, all the other three MCA's retained the reactivity with the antigen in the presence of Ca2+ even after the Gla-domain had been removed. The binding of these MCA’s to PC in the presence of Ca2+ was found to be saturable with respect to the Ca2+ concentration and the half maximal binding for each MCA was calculated to be about 0.5+mM. Moreover, many other divalent cations such as Mg2+, Mn2+ , Ba2+, Zn2+, Co2+, Sr2+, were found to substitute for Ca2+ in inducing the metal ion-dependent but Gla-domain-independent conformer of PC.Cross-reactivity to other vitamin K-aependent plasma proteins was examined by direct ELISA; HPC-2 and 3 reacted solely to PC, but HPC-1 and 4 also reacted with prothrombin and HPC-5 with both prothrombin and factor X.These findings indicated that there are two or more metal binding sites besides the Gla-domain, possibly one in the light chain and the other(s) in the heavy chain. The presence of these metal binding sites may contribute to the unique conformer of vitamin K-dependent plasma proteins including protein C.

Hepcidin, the hormone of iron metabolism, is bound specifically to α-2-macroglobulin in blood

Blood ◽  
2009 ◽  
Vol 113 (24) ◽  
pp. 6225-6236 ◽  
Author(s):  
Gabriela Peslova ◽  
Jiri Petrak ◽  
Katerina Kuzelova ◽  
Ivan Hrdy ◽  
Petr Halada ◽  
...  
Keyword(s):  
Iron Metabolism ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Effector Functions ◽  
High Affinity ◽  
Α2 Macroglobulin ◽  
Novel Drugs ◽  
J774 Cells ◽  
Binding Curve

Abstract Hepcidin is a major regulator of iron metabolism. Hepcidin-based therapeutics/diagnostics could play roles in hematology in the future, and thus, hepcidin transport is crucial to understand. In this study, we identify α2-macroglobulin (α2-M) as the specific hepcidin-binding molecule in blood. Interaction of 125I-hepcidin with α2-M was identified using fractionation of plasma proteins followed by native gradient polyacrylamide gel electrophoresis and mass spectrometry. Hepcidin binding to nonactivated α2-M displays high affinity (Kd 177 ± 27 nM), whereas hepcidin binding to albumin was nonspecific and displayed nonsaturable kinetics. Surprisingly, the interaction of hepcidin with activated α2-M exhibited a classical sigmoidal binding curve demonstrating cooperative binding of 4 high-affinity (Kd 0.3 μM) hepcidin-binding sites. This property probably enables efficient sequestration of hepcidin and its subsequent release or inactivation that may be important for its effector functions. Because α2-M rapidly targets ligands to cells via receptor-mediated endocytosis, the binding of hepcidin to α2-M may influence its functions. In fact, the α2-M–hepcidin complex decreased ferroportin expression in J774 cells more effectively than hepcidin alone. The demonstration that α2-M is the hepcidin transporter could lead to better understanding of hepcidin physiology, methods for its sensitive measurement and the development of novel drugs for the treatment of iron-related diseases.

Bindings of plasma proteins to streptococci of serological group L with special reference to their immunoglobulin G Fc-receptor activity

1988 ◽  
Vol 34 (1) ◽  
pp. 1-5 ◽  
Author(s):  
C. Lämmler ◽  
P. Schaufuß ◽  
C. Frede ◽  
H. Blobel
Keyword(s):  
Affinity Chromatography ◽  
Special Reference ◽  
Molecular Mass ◽  
Immunoglobulin G ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Fc Receptors ◽  
Streptococcus Dysgalactiae ◽  
Serological Group ◽  
Ig G

Of 33 streptococcal cultures belonging to serological group L, all bound human immunoglobulin (Ig) G, fibrinogen, and fibronectin; 32 bound bovine IgG; 31 bound α2-macroglobulin; 5 bound albumin; and none bound either haptoglobin or IgA. The binding sites for IgG could be isolated from the L streptococci by trypsinization and purified by affinity chromatography on human IgG – Sepharose®. The purified Fc receptors reacted with IgG subclasses 1, 2, 3, 4 of humans, 1 and 2 of bovines, ovines, and caprines as well as a, b, c, and T of equines. They had a molecular mass of approximately 49 000 Da. Thus, the Fc receptors from L streptococci corresponded to type III Fc receptors of Streptococcus dysgalactiae.

scholarly journals Interaction Between Rabbit Erythroblast Ferritin and Normal Plasma Proteins

Blood ◽  
1974 ◽  
Vol 43 (6) ◽  
pp. 875-883 ◽  
Author(s):  
Hideo Yamada ◽  
Thomas G. Gabuzda ◽  
Marion Berenfeld
Keyword(s):  
Ionic Strength ◽  
Guinea Pig ◽  
Plasma Proteins ◽  
Starch Granule ◽  
Binding Activity ◽  
The Other ◽  
Heat Stable ◽  
Normal Plasma ◽  
Low Ionic Strength ◽  
Plasma Factors

Abstract Erythroblast ferritin (EF), isolated from phenylhydrazine-anemic rabbit marrow, interacts with components of normal plasma and forms a complex separable by starch granule electrophoresis and by dialysis techniques. The binding is facilitated at low ionic strength. The plasma factors responsible for binding EF are present in autologous, as well as homologous, plasma of normal nonimmune rabbits, although binding activities are quite variable in different plasmas. The binding activity for rabbit EF is also present in heterologous plasma of mouse, guinea pig, and man. The active principles in plasma were identified as two heat-stable components which fractionate as immunoglobulins, one as IgG and the other as IgM. The results support the hypothesis that natural antiferritin antibodies of low titer are present in normal plasma.

scholarly journals Comparison of the dimensions of the combining sites of the dinitrophenyl-binding immunoglobulin A myeloma proteins MOPC 315, MOPC 460 and XRPC 25 by spin-label mapping

1977 ◽  
Vol 165 (2) ◽  
pp. 199-206 ◽  
Author(s):  
Keith J. Willan ◽  
Derek Marsh ◽  
Christopher A. Sunderland ◽  
Brian J. Sutton ◽  
Simon Wain-Hobson ◽  
...  
Keyword(s):  
Binding Sites ◽  
Immunoglobulin A ◽  
Binding Activity ◽  
The Other ◽  
Spin Labels ◽  
Metal Site ◽  
Myeloma Proteins ◽  
Spin Resonance ◽  
Mouse Immunoglobulin ◽  
Positively Charged

The mouse immunoglobulin A myeloma proteins MOPC 315, MOPC 460 and XRPC 25 all possess dinitrophenyl (Dnp)-binding activity. Differences in specificities were shown by measuring the affinities of a variety of haptens. By using a series of Dnp-spin-labelled haptens, the dimensions of the binding sites of the three myeloma proteins were compared by the method described for protein MOPC 315 [Sutton, Gettins, Givol, Marsh, Wain-Hobson, Willan & Dwek (1977) Biochem. J.165, 177–197]. The dinitrophenyl ring is rigidly held in all three sites. The depths of the sites are all 1.1–1.2nm, but there are differences in the lateral dimensions at the entrance to the sites. For protein XRPC 25 these dimensions are 0.75nm×0.8nm, which may be compared with 0.85nm×1.1nm for protein MOPC 315 and ≥1.0nm×1.1nm for protein MOPC 460. The site in protein MOPC 460 is more symmetrical with respect to the plane of the dinitrophenyl ring than in either of the other two myeloma proteins and also allows greater penetration of solvent. In protein XRPC 25 a positively charged residue was located at the entrance to the site, similarly positioned to that reported for protein MOPC 315 [Sutton, Gettins, Givol, Marsh, Wain-Hobson, Willan & Dwek (1977) Biochem. J.165, 177–197]. All three proteins possess lanthanide-binding sites, but only in protein MOPC 315 is there antagonism between lanthanide and hapten binding. However, the effects of the diamagnetic La(III) on the electron-spin-resonance spectra of bound Dnp spin labels in both proteins MOPC 460 and XRPC 25 suggest an interaction between the two sites. Comparison of this effect with that caused by the addition of the paramagnetic Gd(III) enables the distance between the lanthanide- and hapten-binding sites to be calculated. In both proteins MOPC 460 and MOPC 315 the metal site is approx. 1.0nm from the nitroxide moiety of the spin-labelled hapten, but in protein XRPC 25 this distance is at least 2.0nm.

Consistency in Latency Measurements and Interpretation of ABR Tracings

1997 ◽  
Vol 6 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Wayne O. Olsen ◽  
Terri L. Pratt ◽  
Christopher D. Bauch
Keyword(s):  
The Other

Multichannel ABR recordings for 30 otoneurologic patients were reviewed independently by three audiologists to assess interjudge consistency in determining absolute latencies and overall interpretation of ABR results. Four months later, the tracings were reviewed a second time to evaluate intrajudge consistency in interpretation of ABR waveforms. Interjudge agreement in marking latencies for waves I, III, and V within 0.2 ms was on the order of 90% or better. Intrajudge consistency was slightly higher. Only rarely did inter- or intrajudge differences in latency measurements exceed 0.3 ms. Agreement in overall interpretation of ABR results as "normal" or "abnormal" was unanimous for 90% of the patients. Across pairs of judges, the agreement for "normal" and "abnormal" classification of the ABR tracings was 97%. Intrajudge consistency for "normal" and "abnormal" categorization of the ABR results was 100% for one judge, 97% for the other two judges.

Soluble Fibrin Complexes and Fibrinogen Heterogeneity in Diabetes mellitus

1980 ◽  
Vol 44 (03) ◽  
pp. 130-134 ◽  
Author(s):  
E B Tsianos ◽  
N E Stathakis
Keyword(s):  
Diabetes Mellitus ◽  
Molecular Weight ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Lower Molecular Weight ◽  
Polyacrylamide Gels ◽  
Soluble Fibrin ◽  
Α2 Macroglobulin ◽  
Patients With Diabetes

SummaryThe presence of soluble fibrin complexes (SFC) measured by gel filtration of plasma on 4% agarose columns, fibrinogen heterogeneity on 3.5% SDS-polyacrylamide gels and the concentrations of several plasma proteins were evaluated in 39 patients with diabetes mellitus (DM) and 19 matched control subjects. A small but significant increase of SFC was found in DM (p<0.01). On individual basis 51.2% of the patients had increased SFC (>M + 2 SD of the controls). Polyacrylamide gel electrophoresis of the SFC showed no evidence of cross-linking or proteolysis. Plasma clots formed in the presence of EDTA and trasylol were analysed in SDS-polyacrylamide gels in a normal and two lower molecular weight fibrin bands (band I, II, III). The percentage of band I fibrinogen was in diabetics (65.3 ± 4.7%) lower than that of the controls (71.8 ± 4.5%) (p < 0.01). Fibrinogen levels, antithrombin III, α1-antitrypsin, α2-macroglobulin and plasminogen were significantly increased in DM. We suggest that in DM there is an enhancement of intravascular fibrin formation and accelerated fibrinogen degradation to lower molecular weight forms.

RHYNCHOLITES AND THE PROBLEM OF NARROW AND BROAD CONCEPTION OF TAXONS

2018 ◽  
pp. 12-17 ◽  
Author(s):  
I. R. Khuzina ◽  
V. N. Komarov
Keyword(s):  
Sexual Dimorphism ◽  
Morphological Characteristics ◽  
Mass Scale ◽  
Individual Variability ◽  
Point Of View ◽  
The Other ◽  
New Taxon ◽  
Artificial System ◽  
Broad Understanding

The paper considers a point of view, based on the conception of the broad understanding of taxons. According to this point of view, rhyncholites of the subgenus Dentatobeccus and Microbeccus are accepted to be synonymous with the genus Rhynchoteuthis, and subgenus Romanovichella is considered to be synonymous with the genus Palaeoteuthis. The criteria, exercising influence on the different approaches to the classification of rhyncholites, have been analyzed (such as age and individual variability, sexual dimorphism, pathological and teratological features, degree of disintegration of material), underestimation of which can lead to inaccuracy. Divestment of the subgenuses Dentatobeccus, Microbeccus and Romanovichella, possessing very bright morphological characteristics, to have an independent status and denomination to their synonyms, has been noted to be unjustified. An artificial system (any suggested variant) with all its minuses is a single probable system for rhyncholites. The main criteria, minimizing its negative sides and proving the separation of the new taxon, is an available mass-scale material. The narrow understanding of the genus, used in sensible limits, has been underlined to simplify the problem of the passing the view about the genus to the other investigators and recognition of rhyncholites for the practical tasks.

Somatoform disorders: diseases of the civilization

2020 ◽  
pp. 25-30
Author(s):  
I. Kukhtevich
Keyword(s):  
Health Professionals ◽  
Somatoform Disorders ◽  
Neuropsychiatric Disorders ◽  
The Other ◽  
Significant Part ◽  
Organic Basis ◽  
Autonomic Disorders ◽  
The One ◽  
Somatic Diseases

Functional autonomic disorders occupy a significant part in the practice of neurologists and professionals of other specialties as well. However, there is no generally accepted classification of such disorders. In this paper the authors tried to show that functional autonomic pathology corresponds to the concept of somatoform disorders combining syndromes manifested by visceral, borderline psychopathological, neurological symptoms that do not have an organic basis. The relevance of the problem of somatoform disorders is that on the one hand many health professionals are not familiar enough with manifestations of borderline neuropsychiatric disorders, often forming functional autonomic disorders, and on the other hand they overestimate somatoform symptoms that are similar to somatic diseases.

STUDY OF ORNAMENTS IN HUNTO SULTAN AMAY MOSQUE GORONTALO

ARTic ◽  
2019 ◽  
Vol 4 ◽  
pp. 167-176
Author(s):  
Risti Puspita Sari Hunowu
Keyword(s):  
Qualitative Method ◽  
The Other ◽  
Visual Form ◽  
Research Material ◽  
Other Hand ◽  
The World ◽  
Existing Form ◽  
The City ◽  
Dutch Colonial

This research is aimed at studying the Hunto Sultan Amay Mosque located in Gorontalo City. Hunto Sultan Amay Mosque is the oldest mosque in the city of Gorontalo The Hunto Sultan Amay Mosque was built as proof of Sultan Amay's love for a daughter and is a representation of Islam in Gorontalo. Researchers will investigate the visual form of the Hunto Sultan Amay Mosque which was originally like an ancient mosque in the archipelago. can be seen from the shape of the roof which initially used an overlapping roof and then converted into a dome as well as mosques in the world, we can be sure the Hunto Sultan Amay Mosque uses a dome roof after the arrival of Dutch Colonial. The researcher used a qualitative method by observing the existing form in detail from the building of the mosque with an aesthetic approach, reviewing objects and selecting the selected ornament giving a classification of the shapes, so that the section became a reference for the author as research material. Based on the analysis of this thesis, the form  of the Hunto Sultan Amay mosque as well as the mosques located in the archipelago and the existence of ornaments in the Hunto Sultan Amay Mosque as a decorative structure support the grandeur of a mosque. On the other hand, Hunto Mosque ornaments reveal a teaching. The form of a teaching is manifested in the form of motives and does not depict living beings in a realist or naturalist manner. the decorative forms of the Hunto Sultan Sultan Mosque in general tend to lead to a form of flora, geometric ornaments, and ornament of calligraphy dominated by the distinctive colors of Islam, namely gold, white, red, yellow and green.

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