The somatotrophic axis in young steers: influence of nutritional status and oestradiol-17β on hepatic high-and low-affinity somatotrophic binding sites

1988 ◽  
Vol 116 (2) ◽  
pp. 169-177 ◽  
Author(s):  
B. H. Breier ◽  
P. D. Gluckman ◽  
J. J. Bass
Keyword(s):  
Body Weight ◽  
Nutritional Status ◽  
Binding Site ◽  
Binding Sites ◽  
Dry Matter ◽  
Specific Binding ◽  
Scatchard Analysis ◽  
Binding Studies ◽  
High Affinity ◽  
High Affinity Site

ABSTRACT The binding of bovine GH (bGH) to hepatic membranes obtained from steers on either high (3% dry matter of body weight per day) or low (1% dry matter of body weight per day) planes of nutrition with or without an oestradiol-17β implant was studied (n = 5 per group). Binding studies were performed on both crude membrane homogenates and on 100 000 g microsomal membrane fractions; identical results were obtained using both preparations. In all four groups of animals, linear Scatchard plots were obtained, but following pretreatment of the membranes with MgCl2 to remove endogenously bound hormone, curvilinear plots were obtained in the groups on the high plane of nutrition. Analysis of these curves suggested the presence of a high- and low-affinity binding site, the high-affinity site being fully occupied in the absence of MgCl2 pretreatment. The specific binding of bGH in MgCl2-pretreated crude membranes was greater (P < 0·01) in well-fed steers (14·8 ± 1·6%) than in poorly fed steers (9·8 ± 0·9%). Scatchard analysis showed this to be due to the presence of a high-affinity site (dissociation constant (Kd) = 11·6 ± 3·3 pmol/l) in the well-fed animals only. In addition, there was an increase (P < 0·01) in the affinity, but not in the capacity, of the low-affinity site (Kd = 106·4 ± 22·8 pmol/l in well-fed steers and 197·0 ± 23·8 pmol/l in poorly fed steers). Oestradiol treatment was associated with an increase (P < 0·01) in specific binding at both planes of nutrition, but binding was higher (P < 0·01) in well-fed (24·8 ± 2·9%) than in poorly fed (15·6 ± 3·7%) steers. Scatchard analysis after MgCl2 pretreatment again showed a curvilinear plot at the high and a linear plot at the low nutritional plane. The effect of oestradiol was to increase (P < 0·001) the capacity of the high-affinity site from 1·87 ± 0·61 pmol/100 mg in the control well-fed group to 6·56 ± 1 ·2 pmol/100 mg. The capacity of the low-affinity site was increased (P < 0·01) from 20·1 ± 2·6 to 30·1 ± 3·2 pmol/100 mg in the well-fed group, with a similar change in the poorly fed group. Oestradiol had no effect on the apparent affinity of either binding site. These studies demonstrate a heterogeneity of somatotrophic binding sites of hepatic membranes in steers. The presence of a high-affinity site is determined by nutritional status, whereas oestradiol primarily affects receptor capacity. Thus nutrition and oestradiol have independent and qualitatively different effects on somatotrophic binding. As the rate of weight gain correlated (P < 0·01) with the capacity of the high-affinity site, it is suggested that somatotrophic receptor modulation is a primary factor in the regulation of somatic growth in the ruminant. J. Endocr. (1988) 116, 169–177

ADP-BINDING SITES IN PLATELETS: CHARACTERIZATION BY PHOTOAFFINITY LABELING AND BINDING STUDIES WITH FIXED PLATELETS

1987 ◽  
Author(s):  
J R Jefferson ◽  
J T Harmon ◽  
G A Jamieson
Keyword(s):  
Specific Binding ◽  
Photoaffinity Labeling ◽  
Binding Studies ◽  
Dense Granules ◽  
High Affinity ◽  
High Affinity Site ◽  
Adp Receptors ◽  
Antagonists And Inhibitors ◽  
Spacer Arm ◽  
Formalin Fixed

Attempts to photoaffinity label platelet ADP receptors with 2-azidoADP have not been successful possibly due to the absence of a spacer arm between the nucleotide and the photolabile group. We have synthesized a probe having a long spacer arm by coupling 2-(3-aminopropylthio)-ADP to succinimidyl 4-3H-azidobenzoate. Labeling competable by ADP could not demonstrated with intact platelets. With isolated platelet membranes, three bands (Mr 140,000, 110,000 and 46,000) were labeled that were not competed by ADP while three other bands (Mr 188,000, 92,000 and 51,000) were competable by 100 uM ADP.Another problem in characterizing ADP receptors has been complications due to ADP metabolism and secretion from the dense granules. To avoid this problem we have measured the binding of ADP and analogues to formalin-fixed platelets. ADP bound to two sites (Kl, 0.35 ± 0.04 uM; R1, 160,000 ± 20,000 sites/platelet; K2 7.9 ± 2.0 uM; R2, 400,000 ± 40,000 sites/platelet) with low non-specific binding: these values are in agreement with ADP concentrations required for activation. Affinity at the high affinity site was in the sequence ADP(0.35 uM)=ATP(0.4 uM)›2-MeS.ADP(6.8 uM)› GDP(49 uM) › AMP(360 uM); adenosine did not compete. Binding at the high affinity site was blocked by pMBS (EC50 250 uM) and 5-fluoro-sulfonylbenzoyladenosine (EC50 1 mM). This is the first report of photoaffinity labeling of putative ADP receptors. Our experiments with fixed platelets suggest that they may be useful in testing agonists, antagonists and inhibitors in the absence of complications due to secretion and metabolism.

scholarly journals Powerful Induction of Divergent tgs1-Rv3131 Genes in Mycobacterium tuberculosis Is Mediated by DevR Interaction with a High-Affinity Site and an Adjacent Cryptic Low-Affinity Site

2009 ◽  
Vol 191 (19) ◽  
pp. 6075-6081 ◽  
Author(s):  
Santosh Chauhan ◽  
Jaya Sivaswami Tyagi
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Binding Site ◽  
Binding Sites ◽  
Target Genes ◽  
Promoter Activation ◽  
Transcription Start ◽  
High Affinity ◽  
Synergistic Activation ◽  
Dnase I Footprinting ◽  
High Affinity Site

ABSTRACT DevR activates the transcription of ∼48 genes in response to hypoxia and other stresses and triggers metabolic downshift and dormancy development in Mycobacterium tuberculosis. tgs1 and Rv3131 encode triacylglycerol synthase and a putative nitroreductase, respectively, and both are members of the DevR regulon. This study aimed to understand how a single putative DevR binding site identified previously could sustain powerful induction of divergent tgs1-Rv3131 genes. DNase I footprinting revealed that phosphorylated DevR in fact binds to two sites symmetrically located at −42.5 and −63.5 bp from transcription start points of both genes. DevR first bound to the high-affinity site, P, and cooperatively recruited another DevR molecule to the secondary low-affinity site, S, to activate tgs1-Rv3131 transcription by ∼210- and ∼110-fold, respectively. The presence of a single P site significantly reduced activation of tgs1 expression and abolished Rv3131 activity, reinforcing the requirement of two binding sites for robust expression in both directions. P site inversion abolished tgs1 but not Rv3131 transcription despite DevR occupancy at both sites. The lack of tgs1 expression is most likely due to disruption of its −35 promoter element rather than inversion of the binding site per se. We conclude that (i) an overlap of a DevR binding site and −35 sequence is indispensable for promoter activation, (ii) DevR interaction with two binding sites is obligatory for synergistic activation of tgs1-Rv3131 promoters, and (iii) DevR interaction with binding sites of different affinities offers scope for temporal and differential expression of target genes.

scholarly journals Characterization of inositol 1,4,5-trisphosphate- and inositol 1,3,4,5-tetrakisphosphate-binding sites in rat cerebellum

1991 ◽  
Vol 274 (3) ◽  
pp. 861-867 ◽  
Author(s):  
R A J Challiss ◽  
A L Willcocks ◽  
B Mulloy ◽  
B V L Potter ◽  
S R Nahorski
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Radioligand Binding ◽  
Specific Binding ◽  
Binding Activity ◽  
Inositol Polyphosphate ◽  
Homogeneous Population ◽  
Site Model ◽  
High Affinity ◽  
Pentosan Polysulphate

1. The properties of specific Ins(1,4,5)P3- and Ins(1,3,4,5)P4-binding sites have been compared in a crude ‘P2’ cerebellar membrane fraction. 2. A homogeneous population of [3H]Ins(1,4,5)P3-binding sites was present (KD 23.1 +/- 3.6 nM) at high density (Bmax. 11.9 +/- 1.8 pmol/mg of protein); whereas data obtained for [32P]Ins(1,3,4,5)P4 specific binding were best fitted to a two-site model, the high-affinity binding component (KD 2.6 +/- 0.7 nM) constituted 64.2 +/- 4.3% of the total population and was present at relatively low density (Bmax. 187 +/- 27 fmol/mg of protein). 3. The two high-affinity inositol polyphosphate-binding sites exhibited markedly different pH optima for radioligand binding, allowing the two sites to be independently investigated. At pH 8.0, [3H]Ins(1,4,5)P3 binding was maximal, whereas [32P]Ins(1,3,4,5)P4 specific binding was very low; conversely, at pH 5.0, [32P]Ins(1,3,4,5)P4 binding was maximal, whereas [3H]Ins(1,4,5)P3 binding was undetectably low. 4. Both inositol polyphosphate-binding sites exhibited marked positional and stereo-specificity. Of the analogues studied, only phosphorothioate substitution to form inositol 1,4,5-trisphosphorothioate was tolerated at the Ins(1,4,5)P3-binding site, with only a 2-3-fold loss of binding activity. Addition of a glyceroyl moiety at the 1-phosphate position or addition of further phosphate substituents at the 3- or 6-positions caused dramatic losses in displacing activity. Similarly, complete phosphorothioate substitution of Ins(1,3,4,5)P4 caused an approx. 6-fold loss of binding activity at the [32P]Ins(1,3,4,5)P4-binding site, whereas Ins(1,4,5,6)P4, Ins(1,3,4,6)P4, Ins(1,4,5)P3 and Ins(1,3,4,5,6)P5 were bound at least 100-fold weaker at this site. Therefore, only the phosphorothioate derivatives retained high affinity and selectivity for the two inositol polyphosphate-binding sites. 5. Heparin and pentosan polysulphate were potent but non-selective inhibitors at Ins(1,4,5)P3- and Ins(1,3,4,5)P4-binding sites. N-Desulphation (with or without N-reacetylation) of heparin decreased inhibitory activity at the Ins(1,4,5)P3-, but not at the Ins(1,3,4,5)P4-binding site; however, the selectivity of this effect was only about 4-fold. O- and N-desulphated N-reacetylated heparin was essentially inactive at both sites. 6. The results are discussed with respect to the separate identities of the inositol polyphosphate-binding sites.

PGF2 alpha and PGE2 binding to rat myometrium during gestation, parturition, and postpartum

1990 ◽  
Vol 258 (5) ◽  
pp. E740-E747
Author(s):  
M. Molnar ◽  
F. Hertelendy
Keyword(s):  
Placebo Group ◽  
Binding Sites ◽  
Binding Capacity ◽  
Specific Binding ◽  
Time Dependent ◽  
Scatchard Analysis ◽  
Plasma Progesterone ◽  
High Affinity ◽  
The Third ◽  
Venous Plasma

The specific binding of prostaglandins (PG) F2 alpha and E2 was studied in a rat myometrial membrane-enriched fraction during the latter part of gestation and parturition, as well as in the postpartal period. Tritiated PGE2 and PGF2 alpha binding was specific, saturable, time dependent, and directly proportional to the amount of membrane protein. Scatchard analysis indicated the presence of high-affinity (Kd2) and low-affinity (Kd2) binding sites for both PGs. The affinity of both binding sites for PGF2 alpha and the apparent Kd2 for PGE2 remained essentially the same throughout gestation and post-partially and were similar to nonpregnant rats. The apparent Kd1 of PGE2, however, increased by 10-fold from day 21 of gestation to 1 day postpartum. Although the maximal binding capacity of the high-affinity (Bmax1) and low-affinity (Bmax2) binding sites of PGF2 alpha showed a nonsignificant increase compared with prepartum values, reaching maximal values 12-24 h postpartum, those of PGE2 showed a significant increase on the third day after delivery. The concentration of prostanoids in uterine venous plasma and amniotic fluid increased significantly with approaching parturition, whereas plasma progesterone decreased, raising the estradiol-progesterone ratio 25-fold. After unilateral fetectomy, the binding sites for PGF2 alpha and PGE2 increased significantly compared with the contralateral pregnant horns. Administration of the PG synthetase inhibitor, indomethacin, also increased two- to threefold both PGF2 alpha and PGE2 binding compared with the placebo group, whereas intrauterine administration of PGF2 alpha and PGE2 significantly reduced it.(ABSTRACT TRUNCATED AT 250 WORDS)

THE PRESENCE OF LACTOGEN BUT NOT GROWTH HORMONE BINDING SITES IN THE ISOLATED RAT HEPATOCYTE

1977 ◽  
Vol 74 (2) ◽  
pp. 323-334 ◽  
Author(s):  
A. C. HERINGTON ◽  
N. M. VEITH
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Binding Sites ◽  
Specific Binding ◽  
Female Rats ◽  
Scatchard Analysis ◽  
Hormone Binding ◽  
Binding Studies ◽  
Membrane Function ◽  
Liver Membranes

The binding of 125I-labelled human growth hormone (hGH) and bovine growth hormone (bGH) has been studied in hepatocytes isolated from female rats by perfusion with collagenase in situ. The cells appeared to retain normal membrane function, in that amino acid ([14C]α-aminoisobutyric acid) transport was both saturable and temperature-dependent. Amino acid ([14C]leucine) incorporation into protein was also linear over 3 h and was inhibited by cycloheximide. Binding of 125I-labelled hGH was dependent on time, temperature, hepatocyte concentration and hGH concentration. At 22 °C, binding reached a steady-state after 2·5 h and had a half-life of dissociation of 2–3 h. Hormone specificity studies indicated that binding was specific for hormones with prolactin-like activity (hGH, prolactins) and not for growth hormones themselves (bGH). Scatchard analysis revealed a single class of binding site with a binding capacity of 26·74 ± 3·73 fmol/106 cells and a binding affinity of 1·24 × 109 ± 0·17 × 109 (s.e.m.) l/mol (n = 10). There was a significant sex difference in binding (female > male) and binding was subject to marked regulation by oestrogens (stimulation of binding) and by androgens (inhibition). The lactogen-binding sites, therefore, were comparable in many respects to those previously reported in rat liver membranes. No distinct GH binding sites were demonstrable as shown by the lack of specific binding by 125I-labelled bGH, purified either by Sephadex chromatography or by binding to and elution from GH receptors in rabbit liver membranes. The value of receptor purification of tracer for use in hormone binding studies was indicated by a substantial lowering of non-specific binding.

scholarly journals Binding of dihydrotestosterone to a nuclear-envelope fraction from the male rat liver

1982 ◽  
Vol 202 (1) ◽  
pp. 225-230 ◽  
Author(s):  
Y A Lefebvre ◽  
S J Morante
Keyword(s):  
Heat Treatment ◽  
Nuclear Envelope ◽  
Binding Site ◽  
Rat Liver ◽  
Binding Sites ◽  
Specific Binding ◽  
Male Rat ◽  
Scatchard Analysis ◽  
Female Rat ◽  
Similar Class

Intact nuclear ‘ghosts’ containing small amounts of DNA were obtained from rat liver. Incubation of radiolabelled dihydrotestosterone with isolated nuclear-envelope fraction from male rat liver resulted in specific binding of the dihydrotestosterone to the membranes. Optimal binding occurred at 20 degrees C after 20h incubation. Storage for 2 weeks at -80 degrees C resulted in little loss of specific binding. Scatchard analysis revealed a class of binding sites with a KD of 23.2 nM. Pronase and heat treatment destroyed the binding site. Androgens and glucocorticoids competed for labelled dihydrotestosterone binding to the ghosts, whereas oestrogens did not compete. Castration 24h before preparation of ghosts did not alter the binding site, and a similar class of binding sites was identified on female rat liver nuclear envelopes.

Interactions of some partial agonists with high and low affinity binding sites in β-adrenoceptors

1987 ◽  
Vol 65 (1) ◽  
pp. 18-22 ◽  
Author(s):  
I. Takayanagi ◽  
K. Koike ◽  
A. Nakagoshi
Keyword(s):  
Guinea Pig ◽  
Binding Sites ◽  
Specific Binding ◽  
The Other ◽  
Affinity Binding ◽  
High Affinity ◽  
Partial Agonists ◽  
Significant Difference ◽  
High Affinity Site ◽  
Derivatives Of

Interactions of derivatives of befunolol (BFE-37, BFE-55, and BFE-61), carteolol, and pindolol with β-adrenoceptors were tested in guinea pig isolated taenia caecum. All the drugs used acted as partial agonists on the β-adrenoceptors when compared with isoprenaline, a full agonist. The pA2 values of BFE-61, carteolol, and pindolol were significantly larger than their pD2 values, while there was no significant difference between the pA2 and pD2 values for BFE-37 and BFE-55. The specific binding of [3H]befunolol to microsomal fractions from the guinea pig taenia caecum distinguished two binding sites, high affinity and low affinity sites. Both sites are considered to be bound by 50 nM of [3H]befunolol. Specific 3H binding was displaced by BFE-61, carteolol, and pindolol in a biphasic manner but in a monophasic manner by BFE-37 and BFE-55. Furthermore, [3H]befunolol binding was only partially displaced by BFE-55 but completely displaced by the other drugs used. These results, together with our previous findings, suggest that BFE-61, carteolol, and pindolol discriminate between the two affinity binding sites in the β-adrenoceptors, which are not discriminated between by BFE-37, and further that BFE-55 may bind with only the high affinity site.

The Binding Of Thrombin By Clots Formed From Fragment X

1981 ◽  
Author(s):  
C Y Liu ◽  
H L Nossel ◽  
K L Kaplan
Keyword(s):  
Binding Sites ◽  
Degradation Products ◽  
Average Molecular Weight ◽  
Scatchard Analysis ◽  
Fibrinogen Concentration ◽  
Terminal Portion ◽  
Binding Ratio ◽  
High Affinity ◽  
High Affinity Site ◽  
Fibrinogen Molecule

Previous studies showed that: 1. thrombin was specifically and reversibly bound by fibrin, 2. Scatchard analysis of the data suggested high and low affinity binding sites, and 3. the bound thrombin was quantitatively released following proteolysis of the fibrin by plasmin. In the present study thrombin binding to clots formed from fragment X was studied. The binding of thrombin to fibrin decreased progressively in relation to the original fibrinogen concentration as the fibrin was formed from fibrinogen progressively degraded with plasmin and thus progressively less clottable. Fragment X was then isolated by Sephadex G-200 filtration of partially proteolysed fibrinogen. The fragment X preparation exhibited 76% clottability with thrombin, was heterogeneous with an average molecular weight of 292,000 ±36,000, and contained 2 moles fibrinopeptide A and 0.25 moles fibrinopeptide B per mole. Fibrin formed from clottable fragment X bound thrombin with a molar binding ratio of 0.32 compared to 0.35 for fibrin formed from intact fibrinogen and a binding constant of 7.5 × 105 M-1 compared to 6.6 × 105 M-1 for the high affinity site on fibrin from intact fibrinogen. The data indicate that the NH2-terminal end of the Bβ chain and the COOH-terminal portion of the Aα chain arenot required for high affinity thrombin binding. Because the demonstrated binding is to clottable plasmin degradation products and the molar binding ratio is less than one, it is suggested that the higher affinity thrombin binding site is not present in the fibrinogen molecule but is formed by two or more fibrin molecules present in a polymer.

Characterization and localization of a putative oxytocin receptor in the cervix of the oestrous ewe

1994 ◽  
Vol 142 (3) ◽  
pp. 397-405 ◽  
Author(s):  
E L Matthews ◽  
V J Ayad
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Luteal Phase ◽  
Specific Binding ◽  
Oxytocin Receptor ◽  
Oestrous Cycle ◽  
Secretory Cells ◽  
Cervical Tissue ◽  
High Affinity ◽  
General Decline

Abstract The purpose of the present study was to investigate the presence of high-affinity oxytocin-binding sites (putative oxytocin receptors) in the cervix of the non-pregnant ewe. [3H]Oxytocin binding to the peripheral layers of cervical tissue (comprising the serosal layer and the least dense collagenous and muscular layers) and the remaining dense collagenous cervical tissue were studied separately. [3H] Oxytocin-binding sites were detected in membrane fractions prepared from both of these regions, but binding to the peripheral cervix was variable and binding site concentrations were low, hence these were not characterized further. A high-affinity oxytocin-binding site, having a dissociation constant of 1·8 nmol/l, was characterized in the dense collagenous regions of the cervix of ewes killed during the oestrous period. Similar dissociation constants were determined for [Arg8]-vasopressin and the oxytocin-specific agonist [Thr4, Gly7]-oxytocin in competition studies. [3H] Oxytocin binding to peripheral cervical tissue and to the dense collagenous cervix was generally low or undetectable during the luteal phase, but increased in both tissues around the time of luteolysis. Although specific binding to both tissues was variable during the oestrous period, it was higher at this time than during the luteal phase. [3H] Oxytocin-binding site concentrations were also found to be higher within the inner dense collagenous cervix of oestrous ewes than of pregnant, ovariectomized or anoestrous animals. During the oestrous cycle, oxytocin-binding site concentrations reached a maximum in the dense collagenous cervical tissue on the day of oestrus (141·8 ±44 (s.e.m.) fmol/mg protein), showing a general decline during the following days back to luteal phase values. This compared with concentrations of 513·3 ±132·1 and 216·1 ± 13·9 fmol/mg protein, measured for comparative purposes in endometrial and myometrial membrane preparations, respectively, on the day of oestrus in the same group of ewes. However, in membrane preparations of peripheral cervical tissue higher concentrations were measured on day 14 than on the following 2 days and maximal concentrations were not reached until the day after oestrus (52·7 ± 4·2 fmol/mg protein). Concentrations were maintained at similar values during the subsequent 2 days and significant specific binding was still measurable in both regions of the cervix on day 5. The localization of oxytocin-binding sites within dense collagenous cervical tissue was investigated autoradiographically using the 125I-labelled specific oxytocin receptor antagonist [1(β-mercapto-β,β-cyclopentamethylene propionic acid), 2-(ortho-methyl)-Tyr2, Thr4, Orn8, Tyr9 -NH2]-vasotocin. The only clear specific labelling was localized to the luminal epithelium of the uterine section of the cervix of oestrous ewes, with labelling in ewes in the luteal phase clearly reduced or absent. The results demonstrate the presence of a high-affinity oxytocin-binding site within the cervix of the oestrous ewe which is associated with secretory cells and which undergoes similar changes in concentration during the oestrous cycle to uterine oxytocin receptor sites. The significance of this novel putative site of oxytocin action remains to be established. Journal of Endocrinology (1994) 142, 397–405

scholarly journals The AVR4 Elicitor Protein of Cladosporium fulvum Binds to Fungal Components with High Affinity

2002 ◽  
Vol 15 (12) ◽  
pp. 1219-1227 ◽  
Author(s):  
Nienke Westerink ◽  
Ronelle Roth ◽  
Harrold A. Van den Burg ◽  
Pierre J. G. M. De Wit ◽  
Matthieu H. A. J. Joosten
Keyword(s):  
Binding Site ◽  
Specific Binding ◽  
Proteinase K ◽  
Affinity Binding ◽  
Cladosporium Fulvum ◽  
Binding Studies ◽  
Tomato Plants ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site

The interaction between tomato and the fungal pathogen Cladosporium fulvum complies with the gene-for-gene system. Strains of C. fulvum that produce race-specific elicitor AVR4 induce a hypersensitive response, leading to resistance, in tomato plants that carry the Cf-4 resistance gene. The mechanism of AVR4 perception was examined by performing binding studies with 125I-AVR4 on microsomal membranes of tomato plants. We identified an AVR4 high-affinity binding site (KD = 0.05 nM) which exhibited all the characteristics expected for ligand-receptor interactions, such as saturability, reversibility, and specificity. Surprisingly, the AVR4 high-affinity binding site appeared to originate from fungi present on infected tomato plants rather than from the tomato plants themselves. Detailed analysis showed that this fungus-derived, AVR4-specific binding site is heat- and proteinase K-resistant. Affinity crosslinking demonstrated that AVR4 specifically binds to a component of approximately 75 kDa that is of fungal origin. Our data suggest that binding of AVR4 to a fungal component or components is related to the intrinsic virulence function of AVR4 for C. fulvum.

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