Disease relevance of 3.1

• Chick ciliary ganglion neurons examined under a variety of growth and regulatory conditions in culture displayed a constant ratio of about 2:1 for mAb 35 and Bgt 3.1 binding to cell surface sites [1].
• The defect in replication is apparently a consequence of a deletion in one or more viral genes: the haploid genome of the MC29 virus has a molecular weight of ca. 1.7 X 10(6), whereas the genome of the helper virus MCAV has a molecular weight of ca. 3.1 X 10(6) [2].
• Average counts for nalidixic acid-resistant Salmonella after washing were 3.1 log10 cfu/ mL rinse irrespective of water temperature or chlorine level (P < 0.05) [3].
• 1. Developmental states of the collagen content, distribution and architecture in the pectoralis (PT), iliotibialis lateralis (ITL) and puboischiofemoralis (PIF) muscles of male Red Cornish x New Hampshire (RN, 80 d, body weight 2.9 kg) and normal (3.1 kg) broilers were evaluated [4].
• The acute phase response in chickens challenged after 12 h of activity peaked after 4.6 d with an increase of 24%, whereas the acute phase response in chickens challenged after 12 h of rest peaked after 3.1 d with an increase of 51% [5].

High impact information on 3.1

• The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms [6].
• The myosin/actin ratio (wt/wt) for pure myotube, standard muscle, and fibroblast cultures average 3.1, 1.9, and 1.1 respectively [7].
• The chicken and one of the mouse cDNAs were, respectively, 3.7 and 3.1 kilobase pairs in length, predicted proteins of 752 and 724 amino acids with molecular weights of 84.4 and 81.6 kilodaltons, and hybridized to mRNAs in fibroblasts and tissues of approximately 3.6 and 3.4 kilobases (kb) [8].
• Southern analysis confirmed transgene integration and Northern and Western blotting characterized expression (3.1-fold and 6.9-fold elevations in myocardial mRNA and protein levels, respectively) [9].
• The present findings demonstrate that Bgt 3.1 and mAb 35 recognize the same AChRs on the neurons, and provide information about the stoichiometry of binding and the identity of subunits associated with active sites on the receptor [1].

Chemical compound and disease context of 3.1

• A protein neurotoxin (Bgt 3.1) present as a minor component in the venom of Bungarus multicinctus has been shown previously to block acetylcholine (ACh) sensitivity on chick ciliary ganglion (CG) neurons in cell culture [10].

Biological context of 3.1

• The internalization of Bgt 2.2 binding sites induced by Bgt 3.1 provides an unusual opportunity to study cellular mechanisms by which neurons can regulate the number and distribution of their surface components [10].
• The kinetics and affinity of binding are consistent with those inferred from previous physiological studies for Bgt 3.1 inhibition of receptor function [11].
• Ro 22-4839 was found to potently inhibit MLCK with an IC50 value of 3.1 microM but was unable to inhibit the activity of MLCK rendered Ca2+/calmodulin independent by limited tryptic digestion [12].
• Conversely, the activity showed a biphasic behaviour for cAMP hydrolysis, with Km values of 3.1 and 18.5 microM [13].
• B24/B30 chicks with the highest TPI (3.4) and shortest DTD (34.6) were significantly different from B30/B30 (2.8; 41.6) but not from B24/B24 (3.1; 34.9) suggesting dominance of response of the B24 haplotype over B30 in the absence of B23 [14].

Anatomical context of 3.1

• The first probe is a monoclonal antibody, mAb 35, raised against ACh receptor from Electrophorus electric organ, and the second is an alpha-neurotoxin, Bgt 3.1, purified from B. multicinctus venom. mAb 35 binds specifically to a single class of high-affinity sites on the chromaffin cells in culture [15].
• Low levels of sites may be present in cultures of spinal cord and dorsal root ganglion neurons; no binding is found in cultures of skeletal myotubes or cardiac cells when alpha-bungarotoxin is used to block Bgt 3.1 binding to alpha-bungarotoxin sites [11].
• 9. This type I procollagen cDNA hybridizes in DNA excess to DNA isolated from chicken erythrocytes and from embryonic chick calvaria at a log c0t1/2 of 3.1, demonstrating that procollagen cDNA is complementary to unique gene sequences in both tissues and that procollagen genes are not reiterated [16].
• The k(s) (%/d) in (S-), (S+), (T-) and (T+)-fed birds were 56, 64, 84 and 61 (SEM = 3.7) in duodenum, 51, 52, 75 and 58 in jejunum (SEM = 3.1), 66, 67, 105 and 68 (SEM =7.0) in jejunal mucosa cells, 53, 56, 68 and 50 (SEM = 3.7) in ileum and 52, 45, 118 and 39 (SEM = 20.2) in pancreas, respectively [17].
• Furthermore, in adsorption assays, employing a B15 cross-reacting alloantiserum, trisomic and tetrasomic erythrocytes displayed increased adsorption capabilities (1.6 and 3.1 fold, respectively) compared to disomic control cells [18].

Associations of 3.1 with chemical compounds

• Bgt 3.1 inhibits nicotine-induced catecholamine release from the cells to the same extent and with the same concentration dependence that it modulates the number of mAb 35 sites on the cells [15].
• 3.1 can be seen with fluoresence microscopy using rhodamine-labeled Bgt 2.2 as the probe and by immunological techniques using anti-Bgt 2.2 antiserum to locate the bound 125I-Bgt 2 [10].
• Bgt 3.1 binding to the sites is completely inhibited by each of the cholinergic ligands ACh, carbachol, nicotine, d-tubocurarine, and trimethaphan, but not by alpha-bungarotoxin [11].
• This observation was corroborated in pulse-chase experiments where the calculation of total lipoprotein lipase synthesis, based on the rate of change in enzyme-specific activity during the chase, showed no difference between control (8.13 +/- 3.1) and heparin treatments (9.1 +/- 5.3 ng/h/60-mm dish) [19].
• Prostaglandins D2 and A1 maximally stimulated thymidine incorporation by 4.7- and 3.1-fold but caused significant increases only at 10(-8) M [20].

Other interactions of 3.1

• Half maximal effective concentrations for stimulation of AIB uptake were 0.27 +/- 0.03 nmol/l and 34.8 +/- 3.1 nmol/l for IGF-I and insulin respectively, with maximal stimulation of about 340% of basal [21].
• 9. The profile for chicken recombinant latent TGF-beta 3 is slightly shifted with activation between pH 3.1 and 2.5, and between pH 10.0 and 12 [22].
• Competition studies also demonstrate that 3.1 microM vitellogenin inhibits 50% of control 125I-PV binding, but IgG and bovine serum albumin at concentrations up to 10 microM have no effect on 125I-PV binding [23].
• Lesion VDR had low affinity; Kd 83.9 +/- 20.6 pM compared to 30.0 +/- 2.8, 37.8 +/- 3.1, and 33.0 +/- 4.0 pM (p < 0.001), and low receptor number per cell, 920 +/- 74, compared to 1329 +/- 151, 1664 +/- 167, and 1360 +/- 104 (p < 0.01) in the normal proliferating, normal hypertrophic, and TD proliferating cells, respectively [24].
• Northern gel analysis revealed that three species of calbindin-D28K mRNA (2.0, 2.6 and 3.1 kb) were present a priori in the vitamin D-deficient chick brain and that administration of pharmacological doses (6.5 nmol/animal) of 1,25(OH)2D3 failed to influence their relative abundance [25].

Analytical, diagnostic and therapeutic context of 3.1

• The structure of the octameric histone core of the nucleosome has been determined by x-ray crystallography to a resolution of 3.1 A [26].
• Both cytoplasmic and nuclear hormone-macromolecular complexes sediment at 3.1 S in 0.3 M KC1-sucrose gradients, and agarose gel filtration of the components indicates an apparent molecular weight of 58,000 [27].
• Fluorescence titrations gave dissociation equilibrium constants of 3.1 and 0.6 microM for the binding of chicken cystatin and recombinant human cystatin C respectively to AANS-papain and of 11.9 microM for the binding of chicken cystatin to AEDANS-papain [28].
• The free energy difference between the native and denatured states of the hs variant is 3.1 (GdnHCl, 25 degrees C) to 4.0 (differential scanning calorimetry, 74 degrees C) kcal mol-1 greater than that of WT [29].
• Toxin F focused identically on an isoelectric focusing gel with samples of two similar toxins, bungarotoxin 3.1 and kappa-bungarotoxin [30].

References