长期施肥对玉米生育期土壤微生物量碳氮及酶活性的影响

以小麦-玉米轮作长期肥料定位试验为平台,探讨不同养分管理对玉米生育期塿土微生物量碳、氮和酶活性动态变化的影响。试验包括6个处理,分别为不施肥(CK)、单施氮肥(N)、氮磷配合(NP)、氮磷钾配合(NPK)、NPK+秸秆(SNPK)以及有机肥+NPK(MNPK)。结果表明玉米生育期土壤微生物量碳、氮变化显著。不同施肥管理下土壤微生物量碳、氮的高低显著性分别为MNPK>SNPK、NP、NPK>N、CK。玉米生育期内土壤酶活性也变化显著,蔗糖酶、脲酶和纤维素酶在玉米抽雄期达到活性高峰,而磷酸酶在玉米拔节期出现活性高峰。不同施肥管理对土壤酶活性的影响总体表现为MNPK处理最高,其次为SNPK处理,再次为NPK和NP处理,N和CK处理最低。不同施肥处理间土壤微生物量碳、氮以及酶活性与土壤有机碳、全氮、速效磷水平密切相关。塿土长期施用氮磷或氮磷钾化肥可以提高土壤微生物量碳、氮以及酶活性。一季作物秸秆还田配合氮磷钾化肥与氮磷钾相比有提高土壤微生物量碳、氮以及酶活性的趋势。在等氮量下,有机肥配合化肥与其他施肥模式相比,均显著提升土壤化学肥力因素、微生物量碳氮和酶活性。因此,塿土上建议进行有机无机肥配合以提高土壤肥力,保持土壤生物健康。     

长期施肥对小麦-玉米作物系统土壤颗粒有机碳和氮的影响

通过对华北平原小麦-玉米轮作农田生态系统18年田间施肥试验，研究了长期不同施肥处理对耕层(0～20 cm)土壤颗粒有机碳和氮及矿质结合有机碳和氮的影响.施肥处理包括化肥NPK不同组合（NPK、NP、NK、PK）、全部施用有机肥(OM)、一半有机肥+化肥NPK(1/2OMN)及不施肥(CK)共7个处理.结果表明：各施肥处理均能在不同程度上增加土壤颗粒有机碳和氮及矿质结合有机碳和氮含量，提高土壤颗粒有机碳和氮分配比例及颗粒有机质C/N.施肥处理颗粒有机碳和氮储量较不施肥处理分别增加11.7%～196.8%和13.0%～152.2%，土壤颗粒有机碳对总有机碳储量增加的贡献率为31.5%～67.3%，土壤颗粒有机氮对全氮储量增加的贡献率为14.3%～100.0%；矿质结合有机碳和氮储量较不施肥处理分别增加2.0%～75.0%和0.0%～69.8%.各处理颗粒有机碳和氮及矿质结合有机碳和氮储量均以OM处理最高，且有机肥与化肥NPK配施高于单施化肥各处理，而化肥处理中NPK均衡施用效果最好.说明施用有机肥、有机肥与化肥NPK配施及化肥NPK均衡施用是增加土壤颗粒有机碳和氮及矿质结合有机碳和氮的关键.     

长期施用化肥、猪粪和稻草对红壤水稻土化学和生物化学性质的影响

2005年和2007年分别从望城县已建立27年的肥力定位试验田内采集土壤样品,测定土壤有机碳(TOC)、全N、速效N、速效P、微生物生物量碳、氮(Cmic、Nmic)及土壤呼吸和酶活性,研究长期施用化肥、猪粪和稻草对土壤化学和生物化学性质的影响.结果表明:长期施用化肥、猪粪和稻草处理的土壤pH值与试验前相比均有所下降,电导率(EC)变化不大.化肥与猪粪、稻草配施处理的TOC、全N、速效N、速效P、土壤呼吸、Cmic、Nmic和酶活性均高于不施肥(CK)和单施化肥处理;化肥与猪粪、稻草配施处理的水稻产量也高于单施化肥处理.在研究期间,NK化肥与猪粪、NPK化肥与稻草配施处理的Cmic/TOC大于相应的单施化肥处理.各处理土壤生物化学性质与TOC和养分含量呈正相关(P0.01).猪粪、稻草与化肥长期配合施用能显著改善土壤化学和生物化学性质,提高土壤质量和土壤肥力.     

长期定位施肥下黑土碳排放特征及其碳库组分与酶活性变化

黑土作为承担我国粮食安全与生态安全的重要土壤资源,其碳排放特征与碳库组分变化一直是生态学领域研究的热点。施肥是影响黑土有机碳输入、输出的重要因素,而这需要长时间尺度的探究。为明确长期不同施肥下的土壤碳排放特征及其影响机制,以始于1990年的国家土壤肥力与肥料效益监测网站黑土监测基地-公主岭为研究平台,选取不施肥(CK)、单施氮磷钾肥(NPK)、无机肥配施低量有机肥(NPKM1)、1.5倍的无机肥配施低量有机肥(1.5(NPKM1))、无机肥配施高量有机肥(NPKM2)和无机肥配施秸秆(NPKS)6个处理,探讨了长期不同施肥下土壤碳排放量(CO2-C)与土壤碳库组分包括水溶性有机碳(DOC)、微生物量碳(MBC)、颗粒有机碳(POC)、易氧化有机碳(ROC)及其β-葡萄糖苷酶(BG)、木聚糖酶(BXYL)、纤维素酶(CBH)和乙酰基β-葡萄糖胺酶(NAG)等酶活性变化。结果表明:与CK相比,各施肥处理均可以显著增加黑土土壤碳排放量(P0.05),其中,NPK处理土壤碳排放量约为2633.33 kg/hm~2,显著高出CK处理37.36%;长期有机无机配施(NPKM1、1.5(NPKM1)、NPKM2)显著增加土壤碳排放量71.81%—88.51%,效果最为明显;NPKS显著增加土壤碳排放量56.32%,并且三种长期有机无机配施措施碳排放差异不显著。相对CK处理,有机无机配施的DOC、MBC、POC、ROC均有显著增加(P0.05),各指标分别高出CK处理16.07%—56.34%、128.84%—185.77%、284.15%—497.45%和841.03%—1145.94%,其中1.5(NPKM1)处理效果最好。同时,有机无机配施相对CK处理的NAG、BG、BXYL和CBH活性分别提高了313.22%—452.65%、129.45%—250.74%、159.08%—273.32%和72.21%—193.53%,且以1.5(NPKM1)处理的效果最好。土壤碳排放量与土壤酶活性、土壤活性碳库组分之间的相关性分析结果表明,长期不同施肥措施的土壤碳排放量不但与土壤ROC、DOC、POC、MBC含量呈极显著相关(P0.001),也与土壤BG、NAG、CBH、BXYL酶活性呈极显著相关(P0.001),说明施肥可以通过改变土壤各活性碳库组分含量与土壤微生物活性影响土壤碳排放量。     

长期不同施肥下褐土有机碳储量及活性碳组分

依托辽宁阜新褐土田间施肥定位试验,针对不施肥对照(CK)、单施化肥(NPK)、单施有机肥(M)和有机肥-化肥配施(NPKM)4种不同施肥处理,分析0~20 cm耕层土壤总有机碳(TOC)及关键活性碳组分,旨在为区域土壤合理培肥和农业可持续管理提供科学依据。结果表明:在4种施肥处理中,NPKM处理的土壤总有机碳含量及其储量、微生物生物量碳(MBC)、可溶性有机碳(DOC)、颗粒有机碳(POC)和易氧化有机碳(LOC)含量均比其他3种处理高,较对照分别提高40.5%、38.6%、114.7%、57.5%、103.8%和97.6%,且含有机肥的处理土壤微生物生物量碳明显高于不含有机肥的处理。相关性分析表明,TOC、MBC、DOC、POC以及LOC间呈正显著相关性(P0.05),各组分碳间关系密切。在本试验条件下,长期进行有机肥与化肥配施,对于提升土壤有机碳水平的效果最为显著,是提高土壤肥力最优施肥模式。土壤活性碳组分对施肥措施响应敏感,可以作为土壤总碳水平变化的预警指标。     

长期不同施肥处理对苹果产量、品质及土壤肥力的影响

通过连续7年(2003-2010年)的田间定位试验,研究了不同施肥处理\[不施肥对照,CK;不施N肥只施PK肥,PK;不施P肥只施NK肥,NK;不施K肥只施NP肥,NP;单施NPK化肥,NPK;单施有机肥(猪粪),M;化肥有机肥配施(化肥有机肥氮各占一半),NPKM\]对渭北旱塬富士苹果产量、品质及果园土壤养分含量变化的影响.结果表明: 施肥可以提高苹果产量,连续7年不同施肥处理苹果平均产量较对照提高14.4%～63.8%,各处理苹果年平均产量顺序为:NPKM＞NPK≥M＞NP≥NK＞PK＞CK.NPKM、M、NPK处理随着试验时间的推移,果实可溶性糖、维生素C、可溶性固形物含量呈上升趋势,NPKM、M处理不同年际间波动相对较小;NPKM处理糖酸比5年较对照提高了30.9%,维生素C含量提高了17.5%.长期合理施肥有利于提高土壤有机质,NPKM、M处理0～20 cm土层有机质含量提高幅度最大,分别提高了28.8%和29.3%. NPK、NPKM、M处理土壤各层速效氮、有效磷、速效钾含量较试验前均有显著提高,NPK处理0～20 cm、20～40 cm和40～60 cm土层速效氮含量分别提高了22.7%、37.3%和53.4%.与NPK处理相比,NPKM处理的土壤速效磷含量提高了18.7%,且不同处理土壤速效磷含量上层显著大于下层.
     

长期施肥对土壤微生物量及土壤酶活性的影响

 该文以北京国家褐潮土土壤肥力与肥料效益长期监测基地的长期肥料定位试验为平台,研究了长期不同施肥制度对土壤的生物学特性及其土壤酶的影响。主要研究结果：长期撂荒土壤(15年)的有机质和全氮(TN)的含量、微生物量碳(SMB-C)和氮(SMB-N)、土壤的蔗糖酶、磷酸酶和脲酶活性以及SMB-C/SOC(土壤有机碳)和SMB-N/TN比值都高于种植作物的农田土壤;而其代谢商和容重值低于农田土壤。长期施肥的农田(NPK、NPKM 、NPKS和NPKF),其土壤养分含量、微生物量碳和氮以及土壤蔗糖酶、磷酸酶和脲酶活性均高于不施肥的农田(CK);而小麦(Triticum aestivum)-玉米(Zea mays)→小麦-大豆(Glycine max)复种轮作(NPKF)的农田又高于长期复种连作(NPK)的农田;在施肥处理中(NPK、NPKM、NPKS和NPKF),长期化肥与有机肥配合施用的处理(NPKM )的土壤上述指标高于其它施肥处理(NPK、NPKS和NPKF),但其土壤的代谢商、pH值和容重值较低。     

长期施肥对红壤微生物生物量碳氮和微生物碳源利用的影响

采集湖南省祁阳县红壤长期定位施肥19年的土壤样品,分析长期不同施肥红壤的微生物生物量碳、氮和微生物碳源利用率,以揭示长期施肥对红壤微生物学性状的影响.结果表明:施肥19年后,有机肥单施或与化肥配合施用均显著提高土壤微生物生物量碳、氮和微生物碳源利用率.单施有机肥的土壤微生物生物量碳、氮含量分别为231和81mg·kg-1,化肥有机肥配施分别为148和73mg·kg-1,均显著高于化肥配施秸秆、不施肥和单施化肥;施用有机肥和化肥配施秸秆的土壤微生物生物量氮占全氮的比例平均为6.0%,显著高于单施化肥和不施肥.Biolog-ECO分析中,平均吸光值(AWCD)的大小为:化肥有机肥配施、单施有机肥对照单施化肥、化肥配施秸秆.单施有机肥或与化肥有机肥配施增加了红壤微生物对碳水化合物、羧酸、氨基酸、聚合物、酚类和胺类的碳源利用率;化肥配施有机肥的红壤微生物对聚合物类碳源利用率最高,化肥配施秸秆的红壤微生物对碳水化合物类碳源的利用率最高.表明施用有机肥能显著提高红壤的微生物生物量碳、氮和微生物碳源利用率,提高红壤肥力,保持作物高产.     

不同施肥制度土壤微生物量碳氮变化及细菌群落16S rDNA V3 片段PCR产物的DGGE分析

应用化学分析和变性梯度凝胶电泳（DGGE）技术分离PCR扩增的16S rDNA的方法,研究了不同施肥制度对土壤微生物量碳、氮变化及微生物多样性的影响。结果表明,连续15a长期试验下,土壤微生物量碳（SMB-C）和微生物量氮（SMB-N）的含量大小均为长期撂荒（CK0）土壤高于农田土壤,而在农田土壤中,长期施肥的处理（NPK、NPKM、NPKSt和NPKF）高于长期不施肥处理（CK）,不同的种植制度中,长期复种轮作（NPKF）高于长期复种连作（NPK）;各处理的SMB-C/SOC（土壤有机碳）和SMB-N/TN（全氮）的比值的变化趋势与SMB-C和SMB-N变化一致;从PCR-DGGE分析,长期氮磷钾化肥配施有机肥（NPKM）处理的微生物量碳、氮的含量最高,微生物丰度最高,细菌物种最多,其次为长期撂荒（CK0）,CK处理细菌物种最少。UPGMC聚类分析表明NPK和NPKF处理细菌的群落结构相似,CK和CK0处理细菌的群落结构相似,而NPKM和NPKSt处理细菌的群落结构相似。     

长期施肥对灰漠土生物群落和酶活性的影响

长期定位试验表明:施肥对灰漠土生物类群、酶活性有一定影响,同时生物类群和酶活性也改变了土壤生态环境.(1) 施肥对灰漠土动物个体及类群数的影响显著,长期单施化肥对土壤动物优势度作用较大,化肥配施有机肥丰富了土壤动物组成,化肥配施秸秆有利于增加土壤动物的丰度,尤其是疣跳科和等节跳科动物个体数量增加近10倍,长期不施肥土壤动物均匀性较高,但优势类群数较低;(2)灰漠土微生物组成以细菌为主,特殊微生物生理类群是以固氮菌和氨化细菌数量居多.长期单施化肥不利于土壤微生物生长,几种菌类数量均较低,化肥配施有机物料增加了土壤微生物类群数量,比对照增加15%～44%,长期不施肥土壤微生物数量高于单施化肥处理.(3) 灰漠土自身过氧化氢酶含量较高,蔗糖酶次之.土壤4种酶活性中除过氧化氢酶与土壤养分之间呈负相关以外,其余3种酶活性与土壤速效养分均呈正相关或显著正相关.长期单施化肥土壤脲酶、磷酸酶活性降低,长期不施肥土壤脲酶、磷酸酶活性高于单施化肥处理,化肥配施有机肥或秸秆的土壤脲酶、蔗糖酶、磷酸酶活性比长期不施肥增加了24%～31%.因此,化肥配施有机物料增加了土壤酶活性,加速了土壤熟化,改变了土壤生态环境.     

Relationship between enzyme heterozygosity and quaternary structure

The need for proteins to maintain particular quaternary structures constrains variability in amino acid sequence. Monomeric enzymes are then expected to be more variable than dimeric forms, which in turn are expected to be more variable than tetrameric forms. These predictions are confirmed by analysis of available data on enzyme variation. Theories relating enzyme heterozygosity to metabolic function are discussed in the light of these findings.Financial support for part of the work described in this article was derived from NERC Grant GR3/1558 to J. A. Beardmore.     

Detoxification,antioxidant, and digestive enzyme activities and gene expression analysis of Lymantria dispar larvae under carvacrol

Carvacrol is a terpene compound with various biological activities. However, few studies have specifically focused on its insecticidal activity and mechanism of carvacrol. The larvae of Lymantria dispar are seriously harmful herbivorous insect. This study measured the antifeedant, growth-inhibitory, and toxic effects of carvacrol on L. dispar larvae. To further clarify the insecticidal mechanism of carvacrol, the effects of carvacrol on detoxifying enzymes, antioxidative enzymes, digestive enzyme activities, and the mRNA expression of the above-mentioned enzyme genes were investigated. The results of the study showed that the median lethal concentration (LC₅₀) and the sublethal concentration (LC₂₀) of carvacrol were 1.120 mg/mL and 0.297 mg/mL, respectively, at 72 h. After LC₂₀ treatment of L. dispar larvae for 72 h, food intake and weight gain were significantly lower compared with the control. Enzyme activity assays showed that carvacrol significantly inhibited the activities of carboxylesterase (CarE), glutathione S-transferase (GST), and acetylcholinesterase (AchE), and the inhibition rate of AchE activity was highest (66.51%). Carvacrol also activated the activities of superoxide dismutase (SOD) and catalase (CAT), while it inhibited the activities of lipase (LIP) and amylase (AMS), and first inhibited and then activated protease. In addition, qRT-PCR tests showed that carvacrol affected the mRNA expression levels of CarE, GST, AchE, SOD, CAT, LIP, AMS, and protease. This study helps to clarify the insecticidal mechanism of carvacrol on L. dispar larvae.     

Inducible catalase in Pseudomonas fluorescens

The catalase activity of a non-proliferating suspension of Pseudomonas fluorescens doubled after six hours incubation in a 50 mM phosphate buffer medium (pH 7.3). The same effect was observed in a peptone medium. The increased activity was due to induced enzyme synthesis, and not to activation of preexisting catalase. Induced catalase was separated by electrophoresis from deuterium labelled constitutive catalase. The enzyme was also induced under anaerobic conditions in phosphate buffer or in culture when nitrate was supplied as an electron acceptor. Induction was considerably increased by the addition of various nucleotides and amino acids to the incubation medium.     

Biosynthesis of the C-terminal amide in peptide hormones

Recent developments in the study of peptide amidation are reviewed. The main areas covered are assay procedures, purification of amidating enzymes, co-fact0rs and regulation; mechanism and specificity of the amidating reaction, and multiple forms of the amidating enzyme and glycosylation. Discussion is presented on aspects that are poorly understood and new areas open to investigation are indicated.     

Metal-Induced reversible structural interconversion of human mitochondrial NAD(P)+-dependent malic enzyme

Human mitochondrial NAD(P)+-dependent malic enzyme was strongly inhibited by Lu3+. The X-ray crystal structures indicated a structural change between the metal-free and Lu3+-containing enzymes (Yang Z, Batra R, Floyd DL, Hung HC, Chang GG, Tong L. Biochem Biophys Res Commun 2000;274:440-444). We characterized the reversible slow-binding mechanism and the structural interconversion between Mn2+- and Lu3+-containing human mitochondrial malic enzymes. When Lu3+ was added, the activity of the human enzyme showed a downward curve over time, similar to that of the pigeon enzyme. The rate of the transformation (k(obs)) from the initial rate to the steady-state rate increased hyperbolically with the concentration of Lu3+, suggesting the involvement of an isomerization step. Lu3+ had a much higher affinity for the isomerized form (K*(i,Lu (app)) = 4.8 microM) than that of the native form (K(i,Lu (app)) = 148 microM). When an excess of Mn2+ was added to the Lu3+-inhibited enzyme, assays of the kinetic activity showed an upward trend, indicating reactivation. This result also indicated that the reactivation was a slow process. Fluorescence quenching experiments confirmed that the Lu3+-induced isomerization was completely reversible. The dynamic quenching constants for the metal-free, Mn2+-containing, and Lu3+-containing enzyme were 3.08, 3.07, and 3.8 M(-1), respectively. When the Lu3+-containing enzyme was treated with excess Mn2+, the dynamic quenching constant returned to the original value (3.09 M(-1)). These results indicated that binding of Mn2+ did not induce any conformational change in the enzyme. The open form transformed to the closed form only after substrate binding. Lu3+, on the other hand, transformed the open form into a catalytically inactive form. Excess Mn2+ could replace Lu3+ in the metal binding site and convert the inactive form back into the open form. This reversible process was slow in both directions because of the same but opposite structural change involved.     

Partial purification and kinetic properties of three different d-glucosamine 6-P:N-acetyltransferase forms from human placenta

Three distinct forms of -glucosamine 6-P (Gm 6-P):N-acetyltransferases (EC 2.3.1.4) were partially purified from human placental homogenates by carboxy methyl-Sephadex chromatography. Purification of forms I and II were 13.5-fold, while that of form III was 114-fold. All three forms had a pH optimum value of 9.7 in glycine–NaOH buffer. Enzymes II and III had a K_m value for Gm 6-P of 3.0 mM, which was less than half of that observed for form I (7.1 mM). The corresponding K_m values for acetyl CoA were 0.157 (form I), 0.187 (form II) and 0.280 mM (form III), respectively. Activities of all three forms were inhibited at high concentrations of either substrate. These enzymes were inhibited from 82 to 92% by 2.5 mM p-chloromercuribenzoate. The inhibition was largely reversible by inclusion of 2.5 mM dithiothreitol in the incubation mixtures. There was no requirement for divalent cations, as demonstrated by lack of inhibition of enzyme activity by ethylene diamine tetraacetate. The results are discussed in terms of differences among the enzyme properties of human placental, rodent and porcine liver forms.     

Engineered and Native Coenzyme B12-dependent Isovaleryl-CoA/Pivalyl-CoA Mutase

Adenosylcobalamin-dependent isomerases catalyze carbon skeleton rearrangements using radical chemistry. We have recently demonstrated that an isobutyryl-CoA mutase variant, IcmF, a member of this enzyme family that catalyzes the interconversion of isobutyryl-CoA and n-butyryl-CoA also catalyzes the interconversion between isovaleryl-CoA and pivalyl-CoA, albeit with low efficiency and high susceptibility to inactivation. Given the biotechnological potential of the isovaleryl-CoA/pivalyl-CoA mutase (PCM) reaction, we initially attempted to engineer IcmF to be a more proficient PCM by targeting two active site residues predicted based on sequence alignments and crystal structures, to be key to substrate selectivity. Of the eight mutants tested, the F598A mutation was the most robust, resulting in an ∼17-fold increase in the catalytic efficiency of the PCM activity and a concomitant ∼240-fold decrease in the isobutyryl-CoA mutase activity compared with wild-type IcmF. Hence, mutation of a single residue in IcmF tuned substrate specificity yielding an ∼4000-fold increase in the specificity for an unnatural substrate. However, the F598A mutant was even more susceptible to inactivation than wild-type IcmF. To circumvent this limitation, we used bioinformatics analysis to identify an authentic PCM in genomic databases. Cloning and expression of the putative AdoCbl-dependent PCM with an α₂β₂ heterotetrameric organization similar to that of isobutyryl-CoA mutase and a recently characterized archaeal methylmalonyl-CoA mutase, allowed demonstration of its robust PCM activity. To simplify kinetic analysis and handling, a variant PCM-F was generated in which the αβ subunits were fused into a single polypeptide via a short 11-amino acid linker. The fusion protein, PCM-F, retained high PCM activity and like PCM, was resistant to inactivation. Neither PCM nor PCM-F displayed detectable isobutyryl-CoA mutase activity, demonstrating that PCM represents a novel 5′-deoxyadenosylcobalamin-dependent acyl-CoA mutase. The newly discovered PCM and the derivative PCM-F, have potential applications in bioremediation of pivalic acid found in sludge, in stereospecific synthesis of C5 carboxylic acids and alcohols, and in the production of potential commodity and specialty chemicals.     

酶制剂研制的国内外进展和发展策略

简述了酶工程的研究范围,国际上酶制剂工业发展的研究,特点。概述了近年来我国酶制剂工业发展中存在的问题,包括产品结构,技术含量,研发能力。提出我国酶制剂工业今后发展的一些建议：充分发挥资源优势,加强现代生物技术的应用,调整酶制剂产品的结构。     

Comparative studies of suidatrestin, a specific inhibitor of trehalases

Suidatrestin, isolated from a Streptomyces strain, was characterized as a new trehalase inhibitor. Its inhibitory potential was 7 to 50-fold higher than that of validamycin when tested against insect, fungal and mammalian trehalases. The kinetic properties of suidatrestin were studied in vitro with trehalases from flight muscle mitochondria of the fly, Protophormia terraenovae, from larval midgut of the moth, Spodoptera littoralis, and from porcine kidney, as well as with maltase from yeast. Suidatrestin was inactive on maltase but inhibited all trehalases with IC₅₀ values of 0.08–0.1 μM; K_i values ranged from 0.02 to 0.05 μM. The very low K_i/K_m ratios (3.9×10⁻⁶–4.9×10⁻⁶) indicated excellent in vitro inhibitory action of suidatrestin. When injected into larvae of S. littoralis, suidatrestin required high and repetitive doses which lead to reversible inhibition of larval growth only. Consecutive omission of the inhibitor even stimulated weight increase above that of controls. Significant mortality was achieved at a rather high dose only. Injection of a growth-inhibiting dose of suidatrestin did not change hemolymph osmolality as a measure of sugar concentration. The discrepancy between in vitro and in vivo potency of suidatrestin may be understood once its chemical structure is fully known.