人I型胶原基因第一内含子调节转录的研究

人Ｉ型胶原α１（Ｉ）链（ＣＯＬＩＡ１）基因内含子序列在不同细胞内有不同的转录调节活性,报道了含人ＣＯＬＩＡ１基因内含子Ｉ不同区段（＋５４４～＋８５５和＋８２０～＋１０９３）的重组质粒ｐＳＣＥＰ－ＣＡＴ和ｐＳＣＩＰ－ＣＡＴ的构建并转染人胚肌腱成纤维细胞和Ｔｃａ８１１３舌癌细胞,地高辛标记抗ＣＡＴ－ＥＬＩＳＡ检测结果显示：ｐＳＣＥＰ－ＣＡＴ在两种细胞均获表达;ｐＳＣＩＰ－ＣＡＴ在人成纤维细胞未表达,但     

专一识别脱落酸甲酯的单克隆抗体的制备与应用

专一识别２－顺（Ｓ）ＡＢＡ甲酯的单克隆抗体来源于以ＡＢＡ分子中的１－ＣＯＯＨ为偶联位点合成的免疫原。它与游离态ＡＢＡ和结合态ＡＢＡ葡萄糖酯的交叉反应仅分别为１％与３．５％,而与ＡＢＡ类似物,如２－顺－黄质醛、紫黄质以及ＡＢＡ的２－反式异构体和（Ｒ）－对映体则无交叉反应。利用该抗体建立的高度灵敏和精确的ＡＢＡｍｅ酶联免疫测定法,其检测线性范围为０．０４８～１．５２ｐｍｏｌ。通过ＡＢＡｍｅＥＬＩＳＡ和ＧＡ１＋３ＥＬＩＳＡ分析可知羊蹄叶片衰老与内源ＧＡ１＋３／ＡＢＡ比值的下降有关。     

鸡传染性支气管炎病毒S1基因在昆虫细胞中表达水平初探

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冷驯化提高黄瓜幼苗的耐热性

冷驯化提高黄瓜幼苗的耐热性陈贻竹李晓萍李平（中国科学院华南植物研究所,广州５１０６５０）ＥＮＨＡＮＣＥＭＥＮＴＯＦＨＥＡＴＲＥＳＩＳＴＡＮＣＥＩＮＣＨＩＬＬＩＮＧ┐ＡＣＣＬＩＭＡＴＥＤＣＵＣＵＭＢＥＲＳＥＥＤＬＩＮＧＣｈｅｎＹｉ－ｚｈｕＬｉＸｉａｏ－...     

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P~（53） PROTEIN OVEREXPRESSION IN PREMALIGNANT AND MALIGNANT LESIONS OF ORAL MUCOSA：IMMUNOHISTOCHEMICAL OBSERVATION

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Gas chromatography-mass spectrometry evidence for several endogenous auxins in pea seedling organs

Qualitative analysis by gas chromatography-mass spectrometry (GC-MS) of the auxins present in the root, cotyledons and epicotyl of 3-dold etiolated pea (Pisum sativum L., cv. Alaska) seedlings has shown that all three organs contain phenylacetic acid (PAA), 3-indoleacetic acid (IAA) and 4-chloro-3-indoleacetic acid (4Cl-IAA). In addition, 3-indolepropionic acid (IPA) was present in the root and 3-indolebutyric acid (IBA) was detected in both root and epicotyl. Phenylacetic acid, IAA and IPA were measured quantitatively in the three organs by GC-MS-single ion monitoring, using deuterated internal standards. Levels of IAA were found to range from 13 to 115 pmol g^-1 FW, while amounts of PAA were considerably higher (347–451 pmol g^-1 FW) and the level of IPA was quite low (5 pmol g^-1 FW). On a molar basis the PAA:IAA ratio in the whole seedling was approx. 15:1.Abbreviations IAA 3-indoleacetic acid - 4Cl-IAA 4-chloro-3-indoleacetic acid - IBA 3-indolebutyric acid - IPA 3-indolepropionic acid - PAA phenylacetic acid - GC-MS gas chromatography-mass spectrometry - HPLC high-performance liquid chromatography - PFB pentafluorobenzyl ester - PFBBr pentafluorobenzyl bromide - SIM single-ion monitoring - TMSI trimethylsilyl ester     

Indole-3-acetic acid transport in apical dominance: a quantitative approach. Influence of endogenous and exogenous IAA apical source on inhibitory power of IAA transport

The relationship between the amount of indole-3-acetic acid transported (IAA transport) through the second node of 7-day-old pea seedlings and the degree of inhibition of axillary bud outgrowth at the same node was studied. For both the endogenous apical IAA source (leaves of apical bud) and the exogenous one (lanolin paste containing 0.25–1.0 mg mL^–1 IAA) the slope of linear dependence between inhibition and IAA transport was similar. However, the same IAA transport induced different inhibitions, which were higher for the endogenous source. Moreover, the apical bud induced higher inhibition at the same level of IAA transport when the 4th leaf was present than when it was absent. Apparently, the source of IAA also may regulate the inhibitory power of IAA transported from it. IAA transport appears to consists of active and slightly active one moving along different pathways.Abbreviations a and b coefficients of linear regression of the type y = a+bx; - confidence level of t-test - ELISA enzyme linked immunosorbent assay - GR_1,2 ^e/d growth rate of the lateral bud of experimental/decapitated (control) pea plants at the first and second days after treatment or decapitation - I degree of inhibition of lateral bud outgrowth - IAA indole-3-acetic acid - L_1,2,3 the lengths of lateral bud at 1, 2 or 3rd day after treatment or decapitation of pea plants - n data number - r correlation coefficient - T amount of IAA transported through the second node of pea plant for 3 hours - TIBA 2, 3, 5-triiodobenzoic acid - t-test statistical test used here to compare slopes of linear regressions (y = a+bx) calculated as % MathType!MTEF!2!1!+-% feaafiart1ev1aaatCvAUfeBSjuyZL2yd9gzLbvyNv2CaerbuLwBLn% hiov2DGi1BTfMBaeXatLxBI9gBaerbd9wDYLwzYbItLDharqqtubsr% 4rNCHbGeaGqiVu0Je9sqqrpepC0xbbL8F4rqqrFfpeea0xe9Lq-Jc9% vqaqpepm0xbba9pwe9Q8fs0-yqaqpepae9pg0FirpepeKkFr0xfr-x% fr-xb9adbaqaaeGaciGaaiaabeqaamaabaabaaGcbaGaaeiDaiaabc% cacaqG9aGaaeiiaiaadkgadaWgaaWcbaGaaGymaaqabaGccaqGGaGa% aeylaiaabccacaWGIbWaaSbaaSqaaiaaikdaaeqaaOGaaeiiaiaab+% cacaqGGaWaaOaaaeaacaqGBbaaleqaaOGaaeikaiaabohacaqGLbGa% aeiiaiaadkgadaWgaaWcbaGaaGymaaqabaGccaqGPaWaaWbaaSqabe% aacaqGYaaaaOGaaeiiaiaabUcacaqGGaGaaeikaiaabohacaqGLbGa% aeiiaiaadkgadaWgaaWcbaGaaGOmaaqabaGccaqGPaWaaWbaaSqabe% aacaqGYaaaaOGaaeyxaiaab6caaaa!524A!\[{\text{t = }}b_1 {\text{ - }}b_2 {\text{ / }}\sqrt {\text{[}} {\text{(se }}b_1 {\text{)}}^{\text{2}} {\text{ + (se }}b_2 {\text{)}}^{\text{2}} {\text{]}}{\text{.}}\]     

Presence and Measurement of Imidazoleacetic Acid, a γ-Aminobutyric Acid Agonist, in Rat Brain and Human Cerebrospinal Fluid

Imidazoleacetic acid (IAA) was unequivocally demonstrated in rat brain, human CSF, and human plasma by a gas chromatographic-mass spectrometric method that can reliably quantify as little as 8 pmol, i.e., 1 ng. Owing to tautomerism of the imidazole ring, IAA and [15N, 15N]IAA, the internal standard, each formed two chromatographically distinct isomers after derivatization of the ring nitrogens with either ethyl chloroformate or methyl chloroformate. The isomers of n-butyl(N-ethoxycarbonyl)imidazole acetate and n-butyl(N-methoxycarbonyl)imidazole acetate were identified by analysis with methane chemical ionization and electron impact ionization of molecular and fragment ions. The levels (mean +/- SEM) of free IAA were 140 +/- 14 pmol/g and 2.7 +/- 0.2 pmol/ml in brains of untreated rats and human lumbar CSF, respectively. Mean levels of IAA in brains of anesthetized rats, perfused free of blood, did not differ significantly from mean levels of anesthetized, nonperfused controls or from untreated rats. The source or sources of IAA in brain and CSF are unknown. Because IAA is a potent agonist at gamma-aminobutyrate receptors, it merits examination as a regulator in brain.     

The role of the conversion of IBA into IAA on root regeneration in apple: introduction of a test system

A test system for root regeneration was developed that consists of stem slices of apple shoots (ca. 0.5 mm thick; fresh weight ca. 1 mg). Roots regenerated synchronously without intervening callus formation and without interference with compounds originating from other parts of the plant. Supply of indolebutyric acid (IBA) or indoleacetic acid (IAA) induced maximally an average of 8 or 4.5 roots per slice, respectively. After uptake of IBA, a high degree of conjugation resulted in a recovery of 2.5% as internal free IBA (ca. 2 times the medium concentration). Due to conversion of absorbed IBA into IAA a fraction of 0.4% was recovered as (physiologically active) free IAA. After incubation on medium with IAA, 0.5% of the absorbed hormone was recovered in the free acid form. No conversion of IAA into IBA was observed. Equimolar contents of internal free IAA after incubation on IBA or IAA resulted for IBA in a higher number of roots than for IAA. This means that IBA may also act via internal free IBA or may synergistically modify the action or endogenous synthesis of IAA.Abbreviations BHT butyl hydroxy toluene - EtOH ethanol - FW fresh weight - HAc acetic acid - HPLC high performance liquid chromatography - IAA indoleacetic acid - IAA^int free (internal) IAA in the tissue derived from IBA or IAA uptake - IBA indolebutyric acid - IBA^int free (internal) IBA in the tissue derived from IBA or IAA uptake - MeOH methanol - PAR photosynthetic active radiation - SEM standard error of the mean - TLC thin layer chromatography - UV ultra violet     

Radioimmunoassay for pmol-quantities of indole-3-acetic acid for use with highly stable [125I]- and [3H]IAA derivatives as radiotracers

A radioimmunoassay for the detection of as little as 0.5–1 pmol indole-3-acetic acid (IAA) in unpurified or partially purified plant extracts is described. The assay makes use of either IAA[¹²⁵I]tyrosine methyl ester or [³H]IAA methyl ester as radioactive antigens and IAA methyl ester as the assay standard (measuring range: 1–200 pmol). Levels of extractable IAA in a number of biological samples have been estimated.Abbreviations BSA bovine serum albumin - 2,4-D 2,4-dichlorophenoxy acetic acid - DMF dimethyl formamide - GC-MS gas chromatography-mass spectroscopy - IAA indole-3-acetic acid - RIA radioimmunoassay - SICM selected ion current monitoring - TLC thin layer chromatography - TME tyrosine methyl ester Part 18 in the series: Use of immunoassay in plant science     

Diurnal fluctuations of endogenous IAA content in aralia leaves

Diurnal variations in endogenous IAA levels inFatsia japonica leaves, maintaining constant other external factors such as temperature and relative humidity, were studied. Plants were cultivated in a growth chamber (20 °C, 75 % RH, 16 h photoperiod, 400 µmol m^-2 s^-1 PAR). IAA analyses were carried out by analytical IP-HPLC with on-line spectrofluorimetry. Rhythmic variation of endogenous IAA levels was found. At the onset of the light period the IAA concentration dropped very rapidly from 1070 pmol g^-1 (fr.m.) to 144 pmol g^-1 (fr.m.). This concentration was nearly constant throughout the entire light period. During the subsequent dark period the IAA levels increased again to about 1000 pmol g^-1 (fr.m.) at the end of the dark phase. These results were not confirmed in open field conditions where many other external factors probably influence the endogenous IAA content.     

Comparison of different enzyme immunoassays for measuring indole-3-acetic acid in vegetative citrus tissues

An enzyme-linked immunosorbent assay (ELISA) using polyclonal antibodies, which were raised against indole-3-acetic acid (IAA) conjugated to bovine serum albumin (BSA) via the indolic nitrogen (IAA-N₁-BSA), has been developed. The sensitivity and specificity of these antibodies were compared to those of polyclonal and monoclonal antibodies raised against IAA conjugated to BSA via C₁ of the carboxyl group (IAA-C₁-BSA). The sensitivity of the assays improved in the following order: monoclonal antibodies > antibodies to IAA-C₁-BSA > antibodies to IAA-C₁-BSA. Antibodies against IAA-C₁-BSA had less cross-reactivity to indoles structurally related to IAA, excluding indole-3-pyruvic acid. A rapid and effective method for purification of IAA in citrus tissues before analysis by ELISA is described. Values of IAA in citrus ( Citrus sinensis [L.] Osbeck cv. Shamouti orange) shoot tips obtained with all three antibodies were similar. However, in leaf tissues which contain lower amounts of IAA compared to shoot tips, monoclonal antibodies gave higher values of IAA than polyclonal antibodies. Estimation of free IAA levels in purified extracts of citrus shoot tips, very young leaves, and mature leaves was ca 380, 248, and 74 ng (g fresh weight)⁻¹ respectively.     

Effect of detergents and lipids on transducin photoactivation by rhodopsin.

Rhodopsin samples, isolated using four different extraction procedures, were used to investigate the photodependent activation of the GTPase activity of transducin. A complete inhibition of transducin light-dependent GTP hydrolytic activity was observed when rhodopsin purified in the presence of 1% digitonin, following rod outer segment (ROS) solubilization with 1% 3-[(3-cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS), was used for its activation [0 pmol of inorganic phosphate (Pi) released/min/pmol of rhodopsin]. Rhodopsin, isolated in the presence of 1% digitonin following ROS solubilization with 1% digitonin, was capable of stimulating slightly transducin GTPase activity, with an initial rate of 1 pmol of GTP hydrolyzed/min/pmol of rhodopsin. However, rhodopsin purified in the presence of 0.2% n-dodecyl-beta-D-maltoside (DM), following ROS solubilization with either 1% CHAPS or 1% DM, stimulated the enzymatic activity of transducin in a light-dependent manner, with an initial rate of 5 pmol of Pi released/min/pmol of rhodopsin. Addition of 0.075% egg phosphatidylcholine (PC) to the four different solubilized rhodopsin samples significantly enhanced light-stimulated GTP hydrolysis by transducin, with initial rates increasing from 0 to 1, 1 to 2, and 5 to 30 pmol of Pi released/min/pmol of rhodopsin, respectively. Furthermore, DM-solubilized rhodopsin induced the hydrolysis of the maximum amount of GTP by transducin at 0.0075% PC, while digitonin-solubilized rhodopsin only stimulated the GTPase activity of transducin to a similar value, when the amount of the photoreceptor protein was increased 4-fold and 0.15% PC was added to the assay mixture. These results suggest that the effective photoactivation of transducin by rhodopsin requires phospholipids, which seem to be differentially eliminated with the detergent extraction procedure utilized during ROS membranes solubilization and photopigment isolation.     

Comparison of the inhibitory effects of PYY(3-36) and PYY(1-36) on gastric emptying in rats

We compared the effects of the two molecular forms of the brain-gut peptide YY (PYY), PYY(1-36) and PYY(3-36), on gastric emptying. Unanesthetized rats received 20-min intravenous infusions of rat PYY(1-36) (0, 1.7, 5, 17, 50, 100, 170 pmol x kg(-1) x min(-1)) and rat PYY(3-36) (0, 0.5, 1.7, 5, 17, 50, 100, 170 pmol x kg(-1) x min(-1)), either alone or combined, and gastric emptying of saline was measured during the last 10 min of infusion. For comparison, human PYY(3-36) was administered at 0, 17, and 50 pmol x kg(-1) x min(-1). Gastric emptying was decreased by 11, 24, 26 and 38% in response to 17, 50, 100, and 170 pmol x kg(-1) x min(-1) of rat PYY(1-36); by 10, 26, 41, 53, and 57% in response to 5, 17, 50, 100, and 170 pmol x kg(-1) x min(-1) of rat PYY(3-36); and by 35 and 53% in response to 17 and 50 pmol x kg(-1) x min(-1) of human PYY(3-36), respectively. Estimated ED50s were 470 and 37 pmol x kg(-1) x min(-1) for rat PYY(1-36) and PYY(3-36), respectively. In general, within an experiment, coadministration of PYY(1-36) and PYY(3-36) inhibited gastric emptying by an amount that was comparable to that produced when either peptide was given alone. We conclude that 1) intravenous infusion of PYY(1-36) and PYY(3-36) each produces a dose-dependent inhibition of gastric emptying in rats, 2) PYY(3-36) is an order of magnitude more potent than PYY(1-36) in inhibiting gastric emptying, 3) human PYY(3-36) and rat PYY(3-36) inhibit gastric emptying similarly, and 4) PYY(1-36) and PYY(3-36) do not appear to interact in an additive or synergistic manner to inhibit gastric emptying.     

Determination of carbon monoxide (CO) in rodent tissue: effect of heme administration and environmental CO exposure

Carbon monoxide (CO), produced endogenously during heme degradation, is considered a messenger molecule in vascular and neurologic tissues. To study this role, it is important to determine CO concentration in target tissues pre- and post-perturbations. Here, we describe a sensitive and reproducible method, which is linear and accurate, and provide some examples of its application for quantitation of CO concentrations in tissues pre- and post-perturbations. Tissues from adult rats and mice were sonicated (20% w/w), and volumes representing 0.04-8 mg fresh weight (FW) were incubated at 0 degrees C for 30 min with sulfosalicylic acid. CO liberated into the headspace was quantitated by gas chromatography. Tissue CO concentrations (mean+/-SD, pmol CO/mg FW) were as follows: blood (47+/-10, 45+/-5), muscle (4+/-4, 10+/-1), kidney (5+/-2, 7+/-2), heart (6+/-3, 6+/-1), spleen (11+/-3, 6+/-1), liver (4+/-1, 5+/-1), intestine (2+/-1, 4+/-2), lung (2+/-1, 3+/-1), testes (1+/-1, 2+/-1), and brain (2+/-1, 2+/-0) in untreated rat (n=3) and mouse (n=5), respectively. Between the rat and the mouse, only CO concentrations in the muscle and spleen were significantly different (p0.05). Endogenous CO generation, after administration of heme arginate to mice (n=3), increased CO concentrations by 0-43 pmol/mg FW. Exposure of mice (n=3) to 500 ppm CO for 30 min yielded significantly elevated CO concentrations by 4-2603 pmol/mg FW in all tissues over the native state. While blood had the highest CO concentration for all conditions, muscle, kidney, heart, spleen, and liver, all rich in hemoglobin and/or other CO-binding hemoproteins, also contained substantial CO concentrations. Intestine, lung, testes, and brain contained the lowest CO concentrations.