枯萎病不同抗性黄瓜(Cucumis sativus L.)根系分泌物氨基酸组分与抗病的相关性

以5种对枯萎病不同抗性黄瓜品种为试材,对其根系分泌物氨基酸组分进行测定,并对氨基酸组分与黄瓜品种枯萎病抗病性之间的相关性进行了分析。结果表明：在中抗品种根系分泌中检测到的16种氨基酸：半胱氨酸Cys、苏氨酸Thr、丙氨酸Ala、缬氨酸Val、异亮氨酸Lle、天冬氨酸Asp、亮氨酸Leu、苯丙氨酸Phe、甘氨酸Gly、甲硫氨酸Met、组氨酸His、谷氨酸Glu、酪氨酸Tyr、赖氨酸Lys、丝氨酸Ser和精氨酸Arg。其中的精氨酸在感病品种中没有被检出,组氨酸和精氨酸组分在抗病品种中没有被检出。根系分泌物中总氨基酸含量随品种抗性的增加而降低;精氨酸、丝氨酸和赖氨酸的含量与品种对枯萎病的病情指数呈负相关,其他13种氨基酸组分含量与品种对枯萎病的病情指数呈正相关,其中苯丙氨酸含量与病情指数呈显著正相关。丝氨酸与苯丙氨酸、天冬氨酸、丙氨酸、甘氨酸的比值均与品种对枯萎病的病情指数呈显著负相关,其中Ser／Phe与品种对枯萎病的病情指数呈极显著负相关。     

不同晶型、旋光型氨基酸原料药的红外图谱分析

分析比较了 33种不同来源的氨基酸产品红外图谱的差异 ,其中丝氨酸、门冬氨酸、醋酸赖氨酸、谷氨酸 (白色结晶性粉末 )、苏氨酸、缬氨酸、丙氨酸、亮氨酸、脯氨酸、盐酸组氨酸、盐酸精氨酸、酪氨酸、胱氨酸等 13种与标准图谱完全一致 ;甲硫氨酸、盐酸赖氨酸、甘氨酸、谷氨酸 (白色结晶 )等 4种与标准图谱不一致 ,其原因是 :甘氨酸和谷氨酸由晶型不同造成 ,甲硫氨酸因旋光性不同而造成 ,盐酸赖氨酸与相应的生化试剂图谱一致。     

蛋白质的营养价值

组成人体蛋白质的氨基酸有20多种,其中有8种,即:异亮氨酸、亮氨酸、赖氨酸、甲硫氨酸、苯丙氨酸、苏氨酸、色氨酸和缬氨酸(婴儿还包括组氨酸和精氨酸)在人体内不能合成,必须由食物供给,故称为必需氨基酸。     

蚯蚓活动对土壤氨基酸组分及含量的影响

通过室内培养试验,研究了赤子爱胜蚓(Eisenia foetida)和威廉环毛蚓(Metaphire guillelmi)对土壤氨基酸组分及含量的影响,并探讨了两种不同生活型蚯蚓作用效果的异同。结果表明:蚯蚓活动可显著改变土壤氨基酸含量,爱胜蚓作用下土壤酸解氨基酸和游离氨基酸分别增加5.08 g/kg和7.72 mg/kg,环毛蚓作用下土壤酸解氨基酸和游离氨基酸分别增加3.86 g/kg和4.44mg/kg。各处理酸解氨基酸均以中性氨基酸所占比例为最大(平均51.9%),酸性氨基酸次之(平均23.3%),而含硫氨基酸(平均14.4%)及碱性氨基酸最少(平均10.4%)。各处理游离氨基酸同样以中性氨基酸为主,平均54.4%,而以碱性氨基酸含量最少,平均仅为7.2%。蚯蚓活动并未改变土壤氨基酸可检出种类,各处理分别检测出16种酸解氨基酸和14种游离氨基酸。土壤酸解氨基酸和游离氨基酸组分含量在蚯蚓作用下均有明显改变:加入爱胜蚓后土壤酸解氨基酸组分中天冬氨酸、精氨酸、甲硫氨酸、丙氨酸、赖氨酸和甘氨酸增幅较高,均在85.7%以上,缬氨酸、苏氨酸、丝氨酸、谷氨酸、亮氨酸、酪氨酸和组氨酸增幅较小在40.7%—62.7%间波动;加入环毛蚓后土壤酸解氨基酸组分中甲硫氨酸、赖氨酸、天冬氨酸、酪氨酸和丙氨酸增幅较大,均在71.9%以上,甘氨酸、精氨酸、异亮氨酸增幅适中,分别为56.8%、55.6%和54.9%;丝氨酸、亮氨酸、苏氨酸、谷氨酸、组氨酸和苯丙氨酸增幅最小,均在40%以下;游离氨基酸组分中组氨酸、精氨酸、甘氨酸、亮氨酸、异亮氨酸和丙氨酸在加入爱胜蚓后增加的幅度较大,增幅在150.0%以上,增幅较为缓和的氨基酸组分有天冬氨酸、苏氨酸、丝氨酸、缬氨酸、谷氨酸和苯丙氨酸,介于58.8%—92.1%之间;环毛蚓作用下,天冬氨酸、精氨酸、丝氨酸和异亮氨酸增幅最大,分别为184.2%、173.3%、163.0%和116.6%;苏氨酸、亮氨酸、缬氨酸和甘氨酸增幅较缓,介于52.3%—92.7%之间;谷氨酸、组氨酸、苯丙氨酸、丙氨酸和甲硫氨酸增幅较低,均在33.1%之下;而半胱氨酸在蚯蚓作用下显著降低,降幅为11.8%。对比两种生活型蚯蚓作用效果可知,土壤氨基酸总含量及各组分含量在爱胜蚓和环毛蚓作用下的增加或减少趋势相同(土壤酸解氨基酸组分缬氨酸除外),但改变幅度却存在明显差异,总体而言,爱胜蚓作用效果优于环毛蚓。     

持续性植物状态患者血浆、脑脊液中氨基酸水平的变化

目的：探讨持续性植物状态(PVS)患者脑眷液(CSF)和血浆中氨基酸类物质水平与PVS发病的关系。方法：采用高压液相色谱(HPLC)方法测定。结果:PVS患者血浆中较对照组显著升高的氨基酸有：谷氨酸(Glu)、精氨酸(Arg)。脑眷液中较对照组显著升高的氨基酸有：γ-氨基丁酸(GABA)、丝氨酸(Ser)、酪氨酸(Tyr)、色氨酸(Trp)、赖氨酸(Lys)、胍氨酸(Cit);较对照组显著降低的氨基酸有：胱氨酸(CysT)。结论：CSF中的γ-氨基丁酸、丝氨酸、酪氨酸、色氨酸和赖氨酸等的升高,胱氨酸的降低以及血浆中的谷氨酸、精氨酸的升高可能与PVS的发生和发展过程有关。     

慢性肾炎患者血浆游离氨基酸的改变

<正> 近10年来,许多学者从测定血浆游离氨基酸(Free Amino Acid,FAA)来研究某些内科疾病。其中肾脏疾病引起氨基酸代谢的紊乱,虽然比较复杂,但大致可以分三种情况:(1)肾功能损伤时,常引起甘氨酸(Gly)转变为丝氨酸(Ser),瓜氨酸(Cit)转变为精氨酸(Arg)以及苯丙氨酸(Phe)转变为酪氨酸(tyr)均受阻,所以血浆中甘氨酸,瓜氨酸以及苯丙氨酸等氨基酸浓度升高,而丝氨酸,精氨酸以及酪氨酸等氨基酸浓度降低;(2)慢性肾功能衰竭时,常常因维生素B_6缺乏,易引起支链氨基酸(Barnched chaim AminoAcid,BCAA),包括亮氨酸(Leu),异     

小鼠胚胎体外发育培养基中氨基酸含量变化

通过检测哺乳动物早期胚胎体外发育过程中可以消耗或生成某些氨基酸的含量,可以了解胚胎的发育潜能。利用反相高效液相色谱法(RP-HPLC)检测KSOMaa培养基中17种氨基酸含量的变化,了解昆明小白鼠(Mus musculus)植入前胚胎体外培养过程中氨基酸含量的变化,旨在寻找一种能有效支持昆明小鼠胚胎体外发育的培养基氨基酸组成,优化小鼠胚胎体外培养体系。将180枚原核胚分为9组,体外培养至囊胚,分别于胚胎发育不同时期取样做高效液相色谱分析。这些氨基酸在胚胎发育不同时期的培养基中含量变化可分为5种类型:①在2细胞期增加但在4细胞期、8～16细胞期减少,囊胚期又增加的氨基酸(甘氨酸、亮氨酸、苏氨酸、缬氨酸、苯丙氨酸、酪氨酸);②在胚胎发育各个时期均下降(谷氨酸、甲硫氨酸、精氨酸、组氨酸);③在胚胎发育各个时期均增加(丝氨酸、赖氨酸、丙氨酸);④2细胞期含量减少而在其他时期持续增加(天冬氨酸、脯氨酸、色氨酸);⑤囊胚期减少,其他时期都有增加(异亮氨酸)。     

蓖麻蚕可溶性蛋白质的研究

水文研究了不同发育阶段蓖麻蚕组织中可溶性蛋白质在性质及含量上的变化。在各发育阶段可溶性蛋白质都包含有清蛋白类、球蛋白类及明胶。在化蛹初期, 组织提取液中还发现了初级(月示)和胨。除明胶以外的可溶性蛋白质总量及其中清蛋白类的含量因发育阶段而异:在蛹初期最高, 到羽化前后有显著下降, 球蛋白类的含量在各发育阶段比较稳定。雌雄两性的可溶性蛋白质含量不同, 在羽化前后这种两性差异最为显著, 雌性超过雄性约一倍之多。因此, 在蛹后期及成虫中, 蛋白质的两性差异在性质上比在数量上更为显著。 曾用纸上层析法分析了可溶性蛋白质的氨基酸组分。在各发育阶段, 氨基酸的种类相同, 包括胱氨酸(和半胱氨酸)、赖氨酸、组氨酸、精氨酸、丝氨酸、甘氨酸、天门冬氨酸、谷氨酸、苏氨酸、丙氨酸、脯氨酸、酪氨酸、缬氨酸(和蛋氨酸)、苯丙氨酸、以及亮氨酸(和异亮氨酸)。色氨酸在酸水解过程中被破坏。文中列出不同发育阶段可溶性蛋白质中各种氨基酸的百分含量。老熟幼虫吐丝结茧后, 甘氨酸、丙氨酸、酪氨酸和丝氨酸含量下降。     

Eu3+对山黧豆中的氨基酸及蛋白质代谢作用的研究

对山黧豆(Lathyrus sativus L.)幼苗整株,喷施一定浓度的Eu3+溶液吸收后,对其相关的生理指标进行测试,结果表明与水喷比较,根中丝氨酸、甘氨酸、丙氨酸、蛋氨酸、亮氨酸、脯氨酸、胱氨酸与对照持平,缬氨酸、酪氨酸、苯丙氨酸、组氨酸略有升高外,其余均低于对照;茎中除精氨酸、脯氨酸、色氨酸略高于对照外,其余均低于对照;叶中除蛋氨酸、色氨酸略高于对照外,其余均低于对照.游离氨基酸总量增加时,茎＞根＞叶,减少时,根＜茎＜叶.蛋白质含量经Eu3+ 处理茎中减少,根和叶中增加;水解酶比活性根＞茎＞叶;Na+、K+-ATPase活力却表现根＞茎＞叶的趋势.表明Eu3+ 对山黧豆生理活性代谢起到一定的调节作用.     

Effects of orally administrated amino acids on myofibrillar proteolysis in chicks

We examined the effects of orally administrated amino acids on myfibrillar proteolysis in food-deprived chicks. Plasma N(tau)-methylhistidine concentration, as an index of myofibrillar proteolysis, was decreased by the administration of Glu, Gly, Ala, Leu, Ile, Ser, Thr, Met, Trp, Asn, Gln, Pro, Lys and Arg but not by Asp, Val, Phe, Tyr or His to chicks. Orally administrated Cys was fatal to chicks. These results indicate that oral Glu, Gly, Ala, Leu, Ile, Ser, Thr, Met, Trp, Asn, Gln, Pro, Lys and Arg administration suppressed myofibrillar proteolysis in chicks.     

The primary structure of the β-subunit of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa

The complete amino acid sequence of the β-subunit of protocatechuate 3,4-dioxygenase was determined. The β-subunit contained four methionine residues. Thus, five peptides were obtained after cleavage of the carboxymethylated β-subunit with cyanogen bromide, and were isolated on Sephadex G-75 column chromatography. The amino acid sequences of the cyanogen bromide peptides were established by characterization of the peptides obtained after digestion with trypsin, chymotrypsin, thermolysin, or Staphylococcus aureus protease. The major sequencing techniques used were automated and manual Edman degradations. The five cyanogen bromide peptides were aligned by means of the amino acid sequences of the peptides containing methionine purified from the tryptic hydrolysate of the carboxymethylated β-subunit. The amino acid sequence of all the 238 residues was as follows: ProAlaGlnAspAsnSerArgPheValIleArgAsp ArgAsnTrpHis ProLysAlaLeuThrPro-Asp — TyrLysThrSerIleAlaArg SerProArgGlnAla LeuValSerIleProGlnSer — IleSerGluThrThrGly ProAsnPheSerHisLeu GlyPheGlyAlaHisAsp-His — AspLeuLeuLeuAsnPheAsn AsnGlyGlyLeu ProIleGlyGluArgIle-Ile — ValAlaGlyArgValValAsp GlnTyrGlyLysPro ValProAsnThrLeuValGluMet — TrpGlnAlaAsnAla GlyGlyArgTyrArg HisLysAsnAspArgTyrLeuAlaPro — LeuAspProAsn PheGlyGlyValGly ArgCysLeuThrAspSerAspGlyTyrTyr — SerPheArg ThrIleLysProGlyPro TyrProTrpArgAsnGlyProAsnAsp — TrpArgProAla HisIleHisPheGlyIle SerGlyProSerIleAlaThr-Lys — LeuIleThrGlnLeuTyr PheGluGlyAspPro LeuIleProMetCysProIleVal — LysSerIleAlaAsn ProGluAlaValGlnGln LeuIleAlaLysLeuAspMetAsnAsn — AlaAsnProMet AsnCysLeuAlaTyr ArgPheAspIleValLeuArgGlyGlnArgLysThrHis PheGluAsnCys. The sequence published earlier in summary form (Iwaki et al., 1979, J. Biochem.86, 1159–1162) contained a few errors which are pointed out in this paper.     

Amino acid sequence of seminalplasmin, an antimicrobial protein from bull semen

Analytical ultracentrifugation of highly purified seminalplasmin revealed a molecular mass of 6300. Amino acid analysis of the protein preparation indicated the absence of sulfur-containing amino acids cysteine and methionine. The amino acid sequence of seminalplasmin was determined by manual Edman degradation of peptides obtained by proteolytic enzymes trypsin, chymotrypsin and thermolysin: NH₂-Ser Asp Glu Lys Ala Ser Pro Asp Lys His His Arg Phe Ser Leu Ser Arg Tyr Ala Lys Leu Ala Asn Arg Leu Ser Lys Trp Ile Gly Asn Arg Gly Asn Arg Leu Ala Asn Pro Lys Leu Leu Glu Thr Phe Lys Ser Val-COOH. The number of amino acids according to the sequence were 48, the molecular mass 6385. As predicted from the sequence, seminalplasmin very likely contains two α-helical domains in which residues 8-17 and 40-48 are involved. No evidence for the existence of β-sheet structures was obtained. Treatment of seminalplasmin with the above proteases as well as with amino peptidase M and carboxypeptidase Y completely eliminated biological activity.     

烧伤患者血浆和红细胞游离氨基酸变化及输注氨基酸对其变化的影响

动态测定烧伤患者血浆及红细胞内游离氨基酸的含量 ,探讨输入外源性氨基酸后对血及红细胞内游离氨基酸的影响。以日立 835— 5 0型氨基酸自动分析仪测定烧伤患者血浆及红细胞内游离氨基酸含量。结果发现烧伤患者血浆总游离氨基酸浓度从伤后到 2 1天均显著降低 (P <0 .0 5～ 0 .0 1) ;赖、苯丙和苯丙 酪氨酸比值显著升高 (P <0 .0 5～ 0 .0 1) ;色、组、精、丙、甘、苏、脯和丝氨酸比值显著降低 (P <0 .0 5～ 0 .0 1) ;缬、亮、异亮、酪、胱和支链氨基酸伤后早期降低。烧伤患者红细胞内总游离氨基酸含量不同程度降低 ,其中 1、3、7天降低显著 (P <0 .0 5～ 0 .0 1) ;红细胞内苯丙和苯丙 酪氨酸比值未见显著性升高 ;色、蛋、精、脯氨酸含量很低或基本未测出。输注复合氨基酸注射液后未能显著改善患者血及红细胞内游离氨基酸含量。结果提示烧伤患者红细胞内游离氨基酸含量的变化趋势与血浆游离氨基酸变化趋势基本一致 ;烧伤后红细胞内苯丙氨酸及苯丙 酪氨酸比值有别于血浆变化。本研究条件下补充外源性氨基酸未能显著改变烧伤患者血浆及红细胞内游离氨基酸的含量     

Amino acid sequence of a protease inhibitor isolated from Sarcophaga bullata determined by mass spectrometry.

The amino acid sequence of a protease inhibitor isolated from the hemolymph of Sarcophaga bullata larvae was determined by tandem mass spectrometry. Homology considerations with respect to other protease inhibitors with known primary structures assisted in the choice of the procedure followed in the sequence determination and in the alignment of the various peptides obtained from specific chemical cleavage at cysteines and enzyme digests of the S. bullata protease inhibitor. The resulting sequence of 57 residues is as follows: Val Asp Lys Ser Ala Cys Leu Gln Pro Lys Glu Val Gly Pro Cys Arg Lys Ser Asp Phe Val Phe Phe Tyr Asn Ala Asp Thr Lys Ala Cys Glu Glu Phe Leu Tyr Gly Gly Cys Arg Gly Asn Asp Asn Arg Phe Asn Thr Lys Glu Glu Cys Glu Lys Leu Cys Leu.     

Alanine scanning mutagenesis of a type 1 insulin-like growth factor receptor ligand binding site

The high resolution crystal structure of an N-terminal fragment of the IGF-I receptor, has been reported. While this fragment is itself devoid of ligand binding activity, mutational analysis has indicated that its N terminus (L1, amino acids 1-150) and the C terminus of its cysteine-rich domain (amino acids 190-300) contain ligand binding determinants. Mutational analysis also suggests that amino acids 692-702 from the C terminus of the alpha subunit are critical for ligand binding. A fusion protein, formed from these fragments, binds IGF-I with an affinity similar to that of the whole extracellular domain, suggesting that these are the minimal structural elements of the IGF-I binding site. To further characterize the binding site, we have performed structure directed and alanine-scanning mutagenesis of L1, the cysteine-rich domain and amino acids 692-702. Alanine mutants of residues in these regions were transiently expressed as secreted recombinant receptors and their affinity was determined. In L1 alanine mutants of Asp(8), Asn(11), Tyr(28), His(30), Leu(33), Leu(56), Phe(58), Arg(59), and Trp(79) produced a 2- to 10-fold decrease in affinity and alanine mutation of Phe(90) resulted in a 23-fold decrease in affinity. In the cysteine-rich domain, mutation of Arg(240), Phe(241), Glu(242), and Phe(251) produced a 2- to 10-fold decrease in affinity. In the region between amino acids 692 and 702, alanine mutation of Phe(701) produced a receptor devoid of binding activity and alanine mutations of Phe(693), Glu(693), Asn(694), Leu(696), His(697), Asn(698), and Ile(700) exhibited decreases in affinity ranging from 10- to 30-fold. With the exception of Trp(79), the disruptive mutants in L1 form a discrete epitope on the surface of the receptor. Those in the cysteine-rich domain essential for intact affinity also form a discrete epitope together with Trp(79).     

The primary structure of the COOH-terminal half of cholera toxin subunit A1 containing the ADP-ribosylation site

The sequence of 96 amino acid residues from the COOH-terminus of the active subunit of cholera toxin, A₁, has been determined as PheAsnValAsnAspVal LeuGlyAlaTyrAlaProHisProAsxGluGlu GluValSerAlaLeuGlyGly IleProTyrSerGluIleTyrGlyTrpTyrArg ValHisPheGlyValLeuAsp GluGluLeuHisArgGlyTyrArgAspArgTyr TyrSerAsnLeuAspIleAla ProAlaAlaAspGlyTyrGlyLeuAlaGlyPhe ProProGluHisArgAlaTrp ArgGluGluProTrpIleHisHisAlaPro ProGlyCysGlyAsnAlaProArg(OH). This is the largest fragment obtained by BrCN cleavage of the subunit A₁ (M_r 23,000), and has previously been indicated to contain the active site for the adenylate cyclase-stimulating activity. Unequivocal identification of the COOH-terminal structure was achieved by separation and analysis of the terminal peptide after the specific chemical cleavage at the only cysteine residue in A₁ polypeptide. The site of self ADP-ribosylation in the A₁ subunit [C. Y. Lai, Q.-C. Xia, and P. T. Salotra (1983) Biochem. Biophys. Res. Commun.116, 341–348] has now been identified as Arg-50 of this peptide, 46 residues removed from the COOH-terminus. The cysteine that forms disulfide bridge to A₂ subunit in the holotoxin is at position 91.     

Subcellular distribution of aminoacyl-transfer RNA synthetases in Chinese hamster ovary cell culture

Chinese hamster ovary cells grown in cell culture were broken and fractionated by differential centrifugation. Four principal fractions: nuclear and membrane, microsomal, postribosomal, and supernatant were obtained. The distribution of aminoacyl-tRNA synthetases in these four fractions was determined for all twenty amino acids.It was shown that there is a differential distribution of synthetases. Activities specific for eight amino acids: Ala, Ser, Gly, Cys, His, Arg, Thr and Pro were found mainly in the supernatant fraction. Activities specific for eleven amino acids: Asp, Asn, Glu, Gln, Ile, Leu, Lys, Met, Phe, Tyr and Val were found mainly in the postribosomal fraction. Four activities were found at significant levels in the microsomal fraction: Asp, Phe, Lys and Pro. The nuclear and membrane fraction contained activity for Lys, His, Asp and Thr.Changes in aminoacyl-tRNA synthetase activities in various fractions from preparations made by breaking cells with a membrane-dissociating detergent showed that some of the aminoacyl-tRNA synthetase activities may be membrane bound.     

Formation of mutagens by amino-carbonyl reactions

The formation of mutagens by amino-carbonyl reactions of 20 kinds of amino acid and sugars after heating at 100 degrees C for 10 h was examined by the Ames test. The browned solutions of Gly, Ala, Val, Leu, Ile, Ser, Thr, Gln, Lys X HCl, Arg, Phe, Cys, Met and Pro with Glc caused mutation of Salmonella typhimurium TA100 and/or TA98 with or without S9 mix. The presence of S9 mix increased the mutagenic activity of the browned solutions of Cys and Phe with Glc on TA100 and of those of Gly, Ala, Val, Ile and Cys on TA98, but decreased the activity of other solutions. No revertants of Salmonella were induced by the browned solutions of Trp, Tyr, Asp, Asn, Glu and (Cys)2 with Glc. Among positive browned solutions, Cys, Lys, Arg and Phe had the stronger activity, but their activity was weak compared with that of pyrolysates or chemical mutagens such as Trp-P-1, Trp-P-2 and 4-nitroquinoline-N-oxide. The mutagenic activity of the browned solutions increased with prolongation of heating time and varied with the pH of the reaction mixture. Fru, Gal, Ara, Xyl, Man, Lac and Suc also had the ability to form mutagens in the browning reactions with amino acids.     

Sequences of tryptic peptides containing the five cysteinyl residues of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum

Tryptic peptides which account for all five cysteinyl residues in ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum have been purified and sequenced. Collectively, these peptides contain 94 of the approximately 500 amino acid residues per molecule of subunit. Due to one incomplete cleavage at a site for trypsin and two incomplete chymotryptic-like cleavages, eight major radioactive peptides (rather than five as predicted) were recovered from tryptic digests of the enzyme that had been carboxymethylated with [³H]iodoacetate. The established sequences are: GlyTyrThrAlaPheValHisCys¹Lys TyrValAspLeuAlaLeuLysGluGluAspLeuIleAla GlyGlyGluHisValLeuCys¹AlaTyr AlaGlyTyrGlyTyrValAlaThrAlaAlaHisPheAla AlaGluSerSerThrGlyThrAspValGluValCys¹ ThrThrAsxAsxPheThrArg AlaCys¹ThrProIleIleSerGlyGlyMetAsnAla LeuArg ProPheAlaGluAlaCys¹HisAlaPheTrpLeuGly GlyAsnPheIleLys In these peptides, radioactive carboxymethylcysteinyl residues are denoted with asterisks and the sites of incomplete cleavage with vertical wavy lines. None of the peptides appear homologous with either of two cysteinyl-containing, active-site peptides previously isolated from spinach ribulosebisphosphate carboxylase/oxygenase.