Isolation and analysation of soybean agglutinin-specific binding proteins for erythrocyte membrane in different animal species

As assessed by competitive binding and protein-crosslinking experiments, Drosophila melanogaster cells possess basic fibroblast growth factor (bFGF)-specific binding proteins that are similar to FGF receptors on vertebrate cells in molecular weight and binding affinity; these D. melanogaster cells, however, have no detectable binding proteins for acidic fibroblast growth factor (aFGF). Consistent with the presence of bFGF-specific binding proteins, D. melanogaster cells degrade bFGF but not aFGF. These results indicate the conservation of heparin-binding growth factors and receptors between vertebrates and D. melanogaster.

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Characterization of the exposed carbohydrates on the surface membrane of adult Schistosoma mansoni by analysis of lectin binding

Parasitology ◽

10.1017/s0031182000054986 ◽

1980 ◽

Vol 81 (1) ◽

pp. 1-15 ◽

Cited By ~ 50

Author(s):

A. J. G. Simpson ◽

S. R. Smithers

Keyword(s):

Schistosoma Mansoni ◽

Adult Male ◽

Wheat Germ ◽

Ricinus Communis ◽

Specific Binding ◽

Lectin Binding ◽

Surface Membrane ◽

Soybean Agglutinin ◽

Peanut Agglutinin

SUMMARYThe surface architecture of adult male Schistosoma mansoni was explored using a range of lectins with differing carbohydrate specificities. Highest specific binding was achieved with concanavalin A and the agglutinin of molecular weight 60000 from Ricinus communis; the binding of wheat germ agglutinin was mostly non-specific. Small amounts of peanut agglutinin and soybean agglutinin binding were observed and the binding of these lectins was increased by pre-treating the parasite with neuraminidase. The fucose binding protein of Lotus tetragonolobus failed to bind. These results indicate that mannose and/or glucose, galactose, N-acetyl-glucosamine, N-acetyl-galactosamine and sialic acid are exposed on the surface of the adult male schistosome.

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The induction of a specific protease for insulin-like growth factor binding protein-3 in the circulation during severe illness

Journal of Endocrinology ◽

10.1677/joe.0.1300469 ◽

1991 ◽

Vol 130 (3) ◽

pp. 469-NP ◽

Cited By ~ 125

Author(s):

S. C. Davies ◽

J. A. H. Wass ◽

R. J. M. Ross ◽

A. M. Cotterill ◽

C. R. Buchanan ◽

...

Keyword(s):

Binding Proteins ◽

Specific Binding ◽

Nitrogen Retention ◽

Late Pregnancy ◽

Severe Illness ◽

Igf I ◽

Catabolic State ◽

Specific Protease ◽

Circulating Levels ◽

Igfbp 3

ABSTRACT The insulin-like growth factors (IGF-I and IGF-II) are almost completely bound in the circulation to specific binding proteins (IGFBPs). These IGFBPs appear to play a pivotal role in maintaining circulating levels and modulating the delivery of the IGFs to the tissues. A large proportion of the circulating IGFs are bound with high affinity to one of the binding proteins, IGFBP-3. The mechanism by which these IGFs are transferred from the circulatory pool to the tissue receptors is at present unclear. Recent studies in late pregnancy have demonstrated the presence of specific proteases which may modify the IGFBPs such that their affinities for the IGFs are reduced. In this paper, we have demonstrated the presence of a heat-sensitive cation-dependent proteolytic enzyme specific for IGFBP-3 in the serum of five severely ill patients. The activity of this protease was found to vary in these patients, becoming more apparent during fasting than when studied after commencement of parenteral nutrition, indicating that one of the influencing factors in the activity of this protease is the nutritional intake of the patient. Age- and sex-matched healthy adults were also studied in a similar protocol, but no proteolytic modification of any of the IGFBPs was found in any of the samples examined. As the levels of both IGF-I and IGF-II were found to be low in the patients, the presence of a circulatory protease suggests that this may be an adaptive response to increase the bioavailability of the IGFs and possibly to improve the nitrogen retention and counter the catabolic state in severe illness. Journal of Endocrinology (1991) 130,469–473

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Expression, Affinity, and Functional Characterization of the Specific Binding of Two Putative Pheromone-Binding Proteins in the Omnivorous German Cockroach Blattella germanica

Journal of Agricultural and Food Chemistry ◽

10.1021/acs.jafc.0c02456 ◽

2020 ◽

Vol 68 (47) ◽

pp. 13573-13583

Author(s):

Hong Wang ◽

Yun-Feng Ma ◽

Mei-Mei Wang ◽

Guang-Lei Chen ◽

Youssef Dewer ◽

...

Keyword(s):

Binding Proteins ◽

Specific Binding ◽

Functional Characterization ◽

Blattella Germanica ◽

German Cockroach ◽

Pheromone Binding Proteins ◽

Cockroach Blattella Germanica

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Enhancement by GTP of cAMP binding to hepatic nuclei and cytosol

AJP Cell Physiology ◽

10.1152/ajpcell.1984.246.1.c131 ◽

1984 ◽

Vol 246 (1) ◽

pp. C131-C140 ◽

Cited By ~ 2

Author(s):

E. M. Rosenberg ◽

A. D. Goodman ◽

T. L. Lipinski

Keyword(s):

Binding Proteins ◽

Specific Binding ◽

Photoaffinity Labeling ◽

Deae Cellulose ◽

Nuclear Extract ◽

Liver Cytosol ◽

Nuclear Binding ◽

Low Concentrations ◽

Relative Molecular Weight

In the present study we have demonstrated specific binding of 3H-labeled adenosine 3',5'-cyclic monophosphate (cAMP) to a nuclear extract from rat liver. GTP, GDP, and low concentrations of ATP and ADP increased nuclear binding of [3H]cAMP, and AMP inhibited [3H]cAMP binding. Photoaffinity labeling studies employing [32P]cAMP revealed four nuclear binding proteins [relative molecular weight (Mr) 36,000, 49,000, 54,000 and 57,000]. Unlabeled cAMP decreased [32P]cAMP binding to all four proteins, whereas GTP increased binding to the 57,000 protein. We also observed specific binding of [3H]cAMP in the liver cytosol, which was stimulated by GTP but not by ADP or ATP. Photoaffinity labeling studies of the cytosol in the absence of unlabeled nucleotides revealed three cAMP-binding proteins (Mr 36,000, 49,000, and 54,000). Unlabeled cAMP inhibited binding of [32P]cAMP to all three proteins, whereas in the presence of GTP there was binding of [32P]cAMP to a Mr 57,000 protein. Using DEAE-cellulose, we isolated from the nuclear extract and cytosol a cAMP-binding protein that responded to GTP with an increase in cAMP binding but was unaffected by GDP, ATP, ADP, and AMP. Guanosine imidodiphosphate did not affect cAMP binding, suggesting that the stimulatory effect of GTP may be mediated by phosphorylation. We speculate that alterations in intracellular GTP in vivo may modulate the binding of cAMP to a protein in the nucleus and cytosol.

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A versatile method of identifying specific binding proteins on affinity resins

Analytical Biochemistry ◽

10.1016/j.ab.2006.02.008 ◽

2006 ◽

Vol 352 (1) ◽

pp. 15-23 ◽

Cited By ~ 46

Author(s):

Kiyoshi Yamamoto ◽

Akira Yamazaki ◽

Mikio Takeuchi ◽

Akito Tanaka

Keyword(s):

Binding Proteins ◽

Specific Binding

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Reading RNA methylation codes through methyl-specific binding proteins

RNA Biology ◽

10.4161/rna.28829 ◽

2014 ◽

Vol 11 (6) ◽

pp. 669-672 ◽

Cited By ~ 52

Author(s):

Xiao Wang ◽

Chuan He

Keyword(s):

Binding Proteins ◽

Specific Binding ◽

Rna Methylation

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GTP-binding proteins may stimulate insulin biosynthesis in rat pancreatic islets by enhancing the signal-recognition-particle-dependent translocation of the insulin mRNA poly-/mono-some complex to the endoplasmic reticulum

Biochemical Journal ◽

10.1042/bj2750023 ◽

1991 ◽

Vol 275 (1) ◽

pp. 23-28 ◽

Cited By ~ 7

Author(s):

N Welsh ◽

C Oberg ◽

M Welsh

Keyword(s):

Endoplasmic Reticulum ◽

Binding Proteins ◽

Specific Binding ◽

Signal Recognition Particle ◽

Insulin Biosynthesis ◽

Signal Recognition ◽

Insulin Synthesis ◽

Gtp Binding Proteins ◽

Gtp Binding ◽

Insulin Mrna

We aimed to elucidate the putative role of GTP-binding proteins in the regulation of insulin biosynthesis. For this purpose, freshly isolated rat islets were incubated in the presence of liposomes containing GDP, guanosine 5′-[beta-thio]diphosphate (GDP[S]), GTP, guanosine 5′-[gamma-thio]triphosphate (GTP[S]), guanosine 5′-[beta gamma-methylene]triphosphate (p[CH2]ppG), guanosine 5′[beta gamma-imido]triphosphate (p[NH]ppG) and ATP, and the effects of the liposomal delivery of these substances on rates of biosynthesis of insulin and total protein were determined. Insulin biosynthesis during a 1 h incubation at 1.67 mM-glucose was stimulated by ATP- and GTP[S]-containing liposomes as compared with control liposomes. At 16.7 mM-glucose, only the GTP[S]-containing liposomes stimulated insulin biosynthesis. No inhibition of islet protein and insulin synthesis was observed with GDP-, GDP[S]-, p[CH2]ppG- and p[NH]ppG-containing liposomes. By determining the subcellular distribution of insulin mRNA, it was found that the mRNA content associated with microsomes was increased and that associated with the cytosolic mono-/poly-somes decreased when the islets were incubated with GTP[S]-containing liposomes, resulting in an approximate doubling of the ratio of microsomal to polysomal-associated insulin mRNA. ATP-containing liposomes produced no effects on the association of insulin mRNA with microsomes. By using photoaffinity labelling and immunoprecipitation techniques, specific binding of GTP[35S] to the alpha-subunit of the signal-recognition particle (SRP) receptor in islet homogenates containing physiological concentrations of GTP and GDP was demonstrated. These findings suggest that the GTP-binding subunit(s) of the SRP receptor, and possibly also of other GTP-binding proteins involved in this process, may regulate insulin biosynthesis by stimulating the translocation of insulin mRNA to the endoplasmic reticulum and by increasing preproinsulin-peptide translocation into the lumen of the reticulum.

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