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1.
Qiuxiang Pang Xuemei Liu Bosheng Zhao Wei Wei Xiufang Zhang Lianfei Zhao Jingjing Xie Huanhuan Sun 《Central European Journal of Biology》2012,7(2):354-361
Lectins are important components of the immune defense system of invertebrates. Given their important functions, numerous
investigations have been carried out on the characterization and function of lectins in invertebrates. However, lectin studies
with the freshwater planarian, an evolutionarily important animal, are rare. In this paper, we demonstrate agglutination of
glutaraldehyde treated erythrocytes by a lectin with preference for rabbit erythrocytes. The result of hemagglutinating activity
inhibition assays with several carbohydrates showed the most potent inhibitor was maltose. A natural lectin from the crude
homogenates of freshwater planarian Dugesia japonica was purified by single step affinity chromatography using amylose-coupled agarose. The purified protein appeared as one band
with a molecular mass of 350 kDa in PAGE, and as one band, approximately 56 kDa, in SDS-PAGE. The purified lectin showed dependence
on calcium. The activity of the purified lectin was inhibited at temperatures greater than 50°C and showed a pH optimum between
5–8. The purified lectin also has binding activity to the Gram-negative bacteria E. coli, and the Gram-positive bacteria B. subtilis. Furthermore, the purified lectin obtained from injured and bacteria-induced planarians showed increased agglutinating activity
against rabbit erythrocytes. These results suggest that the purified lectin may play an important role in the innate immunity
of the freshwater planarian. 相似文献
2.
Jong Won Han Min Gui Jung Min Jung Kim Kang Sup Yoon Key Pyoung Lee Gwang Hoon Kim 《Phycological Research》2010,58(2):143-150
A d ‐mannose specific lectin was purified from the green marine alga, Bryopsis plumosa (Huds.) Ag. The lectin agglutinated horse and sheep erythrocytes. Matrix assisted laser desorption/ionization time of flight mass spectrometry, size exclusion chromatography, sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) and two dimensional gel electrophoresis (2DE) results showed that the lectin was a monomer with molecular weight of 17 kDa and pI 7.3. The agglutinating activity was inhibited by d ‐mannose (1 mM), α‐methyl‐D‐mannose (4 mM) and l ‐fucose (8 mM). d ‐glucose (125 mM) showed weak inhibition. The lectin did not need divalent cations for agglutinating activity. N‐terminal amino acid sequence of the lectin was analyzed. As the lectin was novel, we named it BPL‐2 (Bryopsis plumosa lectin 2). Full cDNA sequence of BPL‐2 was obtained using cDNA library. It was comprised of 624 bp of open reading frame and 167 bp/57 bp of 3′/5′ untranslated regions as well as N‐terminal signal peptide. No antimicrobial activity of BPL‐2 was observed in four bacteria strains tested. 相似文献
3.
Syed FB Joshi BN SivaRaman H Khire JM Khan MI 《Biochemistry and molecular biology international》1999,47(3):361-367
A lectin was isolated from Agrobacterium radiobacter cell surface and purified. It is a monomer of 40 kDa as shown by SDS-PAGE. The lectin has a pI of 9.15 and amino acid composition of the lectin shows that 44% of the amino acids are hydrophobic. The lectin agglutinates rabbit erythrocytes but does not agglutinate human erythrocytes. It does not show specificity for monosaccharides except for D-glucosamine. Fetuin and its N-linked glycopeptide also inhibit the activity of the lectin but greater inhibition is shown by locust bean gum and Nicotiana tobaccum (tobacco) tissue extracts. 相似文献
4.
Purification and functional characterization of lectin with phenoloxidase activity from the hemolymph of cockroach,Periplaneta americana
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Ganesh Arumugam Bhuvaragavan Sreeramulu Ramaraj Paulchamy Sakthivel Thangavel Janarthanan Sundaram 《Archives of insect biochemistry and physiology》2017,95(2)
Lectins also identified as hemagglutinins are multivalent proteins and on account of their fine sugar‐binding specificity play an important role in immune system of invertebrates. The present study was carried out on the hemolymph lectin of cockroach, Periplaneta americana with appropriate screening and purification to understand its molecular as well as functional nature. The lectin from the hemolymph was purified using ion‐exchange chromatography. The approximate molecular weight of purified lectin was 340 kDa as determined by FPLC analysis. Rabbit erythrocytes were highly agglutinated with purified lectin from the hemolymph of P. americana. The hemagglutination activity (HA) of lectin was specifically inhibited by fucose. Glycoproteins also inhibited the HA activity of lectin. The amino acid sequences of the purified lectin revealed homology with amino acid sequences of allergen proteins from P. americana. Purified lectin showed the highest phenoloxidase activity against dopamine. The activators such as exogenous proteases and LPS from Escherichia coli and Salmonella minnesota significantly enhanced the PO activity of the purified lectin. Besides, the presence of copper and hemocyanin conserved domain in the purified lectin provided a new facet that insects belonging to the ancient clade such as cockroaches retained some traces of evolutionary resemblance in possessing lectin of ancient origin. 相似文献
5.
Takemi Yatohgo Munehiro Nakata Yoichi Tsumuraya Yohichi Hashimoto Shigeru Yamamoto 《Bioscience, biotechnology, and biochemistry》2013,77(6):1485-1493
A lectin was purified to homogeneity from the fruitbodies of Flammulina velutipes by conventional purification procedures. The purified lectin was demonstrated to be a dimeric protein consisting of two identical subunits with an apparent molecular mass of 11 kDa. The lectin was an acidic protein with a pI value of 5.4, and devoid of cysteine, methionine, and histidine as amino acid constituents. Its hemagglutinating activity was totally unaffected by mono- and oligosaccharides and glycosides, but inhibited by some desialylated glycoproteins. Immunological assays revealed that no protein cross-reacting with rabbit anti-i7. velutipes lectin antibody was apparently present in vegetatively growing mycelia but was distributed throughout the fruitbody at different concentrations. 相似文献
6.
Wanida Rittidach Nisa PaijitPrapaporn Utarabhand 《Biochimica et Biophysica Acta (BBA)/General Subjects》2007
A lectin from the hemolymph of the banana shrimp Fenneropenaeus merguiensis was purified by affinity chromatography on a fetuin-agarose column following by gel filtration on a Superose-12 column. The native molecular mass of purified F. merguiensis lectin (FmL) determined by gel filtration was 316.2 kDa and its carbohydrate content was estimated to be 4.4%. By SDS-PAGE analysis, purified FmL consisted of 32.3 kDa and 30.9 kDa subunits. These data suggest that this lectin is an oligomer. Two-dimensional electrophoresis showed that it had a pI value of 6.0 and was mainly composed of glycine, serine, histidine, glutamic acids and glutamine, with relatively lower amounts of methionine and tyrosine. Purified FmL expressed higher agglutination activity against rabbit and rat erythrocytes than with those from human, and its activity was Ca2+-dependent. The hemagglutinating activity of FmL was stable up to 55 °C and at pH 7.5–8. N-acetylated sugars, such as ManNAc, GlcNAc, GalNAc, and NeuNAc were strong inhibitors of the FmL induced hemagglutinating activity with NeuNAc being most effective. Porcine stomach mucin and fetuin were the most potent inhibitors of FmL. Purified FmL caused selective agglutination of Vibrio harveyi, and Vibrio parahemolyticus both pathogens of this Penaeus species and to a lesser extent Vibrio vulnificus but had no effect on the non-pathogenic strains; Vibrio cholerae, Salmonella typhi and Escherichia coli. Its bacterial agglutination was also completely inhibited by NeuNAc, mucin, fetuin and also anti-FmL antibody. This observation indicates that FmL may contribute to the defense response of this species of penaeid shrimps to potentially pathogenic bacteria. 相似文献
7.
Upadhyay SK Saurabh S Singh R Rai P Dubey NK Chandrashekar K Negi KS Tuli R Singh PK 《The protein journal》2011,30(6):374-383
A lectin was purified from the leaves of Allium altaicum and corresponding gene was cloned. The lectin namely Allium altaicum agglutinin (AAA) was ~24 kDa homodimeric protein and similar to a typical garlic leaf lectin. It was synthesized as 177 amino
acid residues pre-proprotein, which consisted of 28 and 43 amino acid long N and C-terminal signal peptides, respectively.
The plant expressed this protein more in scapes and flowers in comparison to the bulbs and leaves. Hemagglutination activity
(with rabbit erythrocytes) was 1,428 fold higher as compared to Allium sativum leaf agglutinin (ASAL) although, the insecticidal activity against cotton aphid (Aphis gossypii) was relatively low. Glycan array revealed that AAA had higher affinity towards GlcAb1-3Galb as compared to ASAL. Homology
analysis showed 57–94% similarity with other Allium lectins. The mature protein was expressed in E. coli as a fusion with SUMO peptide in soluble and biologically active form. Recombinant protein retained high hemagglutination activity. 相似文献
8.
Blackgram (Vigna mungo
L. Hepper)seeds contain two galactose-specific lectins, BGL-I and BGL-II. BGL-I was partially purified into two monomeric lectins which
were designated as BGL-I-1 (94 kDa) and BGL-I-2 (89 kDa). BGL-II is a monomeric lectin of 83 kDA. The purified lectins were
associated with galactosidase activities. BGL-I-1 and BGL-II were copurified with α-galactosidase activity while BGL-I-2 was
largely associated with β-galactosidase activity. These lectins agglutinate trypsin treated rabbit erythrocytes, but not the
human erythrocytes of A, B or O groups. They were stable between pH 3·5 and 7·5 for their agglutination. The lectins did not
show any metalion requirement. They were inactivated at 50°C. The lectin activity was inhibited by D-galactose (0·1 mM). The
Scatchard plots of galactose binding to these lectins are nonlinear and biphasic curves indicative of multiple binding sites.
The data show that the monomeric lectins have both lectin and galactosidase activities suggestive of a bifunctional protein. 相似文献
9.
Oliveira MD Andrade CA Santos-Magalhães NS Coelho LC Teixeira JA Carneiro-da-Cunha MG Correia MT 《Letters in applied microbiology》2008,46(3):371-376
Aims: The aim of this work was to analyse the antimicrobial properties of a purified lectin from Eugenia uniflora L. seeds. Methods and Results: The E. uniflora lectin (EuniSL) was isolated from the seed extract and purified by ion‐exchange chromatography in DEAE‐Sephadex with a purification factor of 11·68. The purified lectin showed a single band on denaturing electrophoresis, with a molecular mass of 67 kDa. EuniSL agglutinated rabbit and human erythrocytes with a higher specificity for rabbit erythrocytes. The haemagglutination was not inhibited by the tested carbohydrates but glycoproteins exerted a strong inhibitory action. The lectin proved to be thermo resistant with the highest stability at pH 6·5 and divalent ions did not affect its activity. EuniSL demonstrated a remarkable nonselective antibacterial activity. EuniSL strongly inhibited the growth of Staphylococcus aureus, Pseudomonas aeruginosa and Klebsiella sp. with a minimum inhibitory concentration (MIC) of 1·5 μg ml?1, and moderately inhibited the growth of Bacillus subtilis, Streptococcus sp. and Escherichia coli with a MIC of 16·5 μg ml?1. Conclusions: EuniSL was found to be effective against bacteria. Significance and Impact of the Study: The strong antibacterial activity of the studied lectin indicates a high potential for clinical microbiology and therapeutic applications. 相似文献
10.
N. A. Hoang B. B. Berezin V. M. Lakhtin I. A. Yamskov 《Applied Biochemistry and Microbiology》2001,37(5):534-537
A lectin was isolated from the venom of scorpion Buthus occitanussp. by means of Sephadex G-50 gel filtration and CM-cellulose ion exchange chromatography. The homogeneous lectin preparation consisted of homodimeric molecules with a subunit M
rof 9.3 kDa. Glycine, alanine, and serine dominated in the lectin amino acid composition. The lectin was a glycoprotein containing 20% carbohydrates (predominantly mannose and glucose). Trypsin-treated murine erythrocytes agglutinated at a lectin concentration of 32 g/ml. Hemagglutination was inhibited by carbohydrates (L-fucose > D-glucose > L-rhamnose > D-xylose). The lectin revealed no phospholipase or hyaluronidase, nor toxic activity. 相似文献
11.
A lectin from the hemolymph of the banana shrimp Fenneropenaeus merguiensis was purified by affinity chromatography on a fetuin-agarose column following by gel filtration on a Superose-12 column. The native molecular mass of purified F. merguiensis lectin (FmL) determined by gel filtration was 316.2 kDa and its carbohydrate content was estimated to be 4.4%. By SDS-PAGE analysis, purified FmL consisted of 32.3 kDa and 30.9 kDa subunits. These data suggest that this lectin is an oligomer. Two-dimensional electrophoresis showed that it had a pI value of 6.0 and was mainly composed of glycine, serine, histidine, glutamic acids and glutamine, with relatively lower amounts of methionine and tyrosine. Purified FmL expressed higher agglutination activity against rabbit and rat erythrocytes than with those from human, and its activity was Ca(2+)-dependent. The hemagglutinating activity of FmL was stable up to 55 degrees C and at pH 7.5-8. N-acetylated sugars, such as ManNAc, GlcNAc, GalNAc, and NeuNAc were strong inhibitors of the FmL induced hemagglutinating activity with NeuNAc being most effective. Porcine stomach mucin and fetuin were the most potent inhibitors of FmL. Purified FmL caused selective agglutination of Vibrio harveyi, and Vibrio parahemolyticus both pathogens of this Penaeus species and to a lesser extent Vibrio vulnificus but had no effect on the non-pathogenic strains; Vibrio cholerae, Salmonella typhi and Escherichia coli. Its bacterial agglutination was also completely inhibited by NeuNAc, mucin, fetuin and also anti-FmL antibody. This observation indicates that FmL may contribute to the defense response of this species of penaeid shrimps to potentially pathogenic bacteria. 相似文献
12.
Dresch RR Zanetti GD Lerner CB Mothes B Trindade VM Henriques AT Vozári-Hampe MM 《Comparative biochemistry and physiology. Toxicology & pharmacology : CBP》2008,148(1):23-30
The lectin from the marine sponge Axinella corrugata (ACL-I) was purified by affinity chromatography on rabbit erythrocytic stroma incorporated into a polyacrylamide gel followed by gel filtration on Ultrogel AcA 44 column. Purified ACL-I is a hexameric glycoprotein with a Mr of 82.3 kDa estimated by SDS-PAGE and 78.5 kDa by FPLC on Superose 12 HR column. The pI of lectin is 6.3 and ACL-I is constituted of 13.9 kDa similar subunits some of them linked by disulphide bridges. This lectin agglutinates native rabbit, goat and dog erythrocytes and in less extent human erythrocytes. The hemagglutinating activity is independent of Ca(2+), Mg(2+) and Mn(2+), but it is strongly inhibited by carbohydrates containing N-acetyl groups. ACL-I is stable up to 70 degrees C for 30 min, with optimum pH between 7 and 8, and it is also resistant to enzymatic proteolysis in vitro. In the presence of reducing or denaturant agents, the lectin activity decreases. ACL-I displays chemotactic effect on rat neutrophil in vitro which is inhibited by N-acetyl-d-glucosamine. 相似文献
13.
Ganapati G. Bhat Kartika N. Shetty Nagaraja N. Nagre Vivek V. Neekhra S. Lingaraju Ramesh S. Bhat Shashikala R. Inamdar K. Suguna Bale M. Swamy 《Glycoconjugate journal》2010,27(3):309-320
A mannose-binding lectin (RVL) was purified from the tubers of Remusatia vivipara, a monocot plant by single-step affinity chromatography on asialofetuin-Sepharose 4B. RVL agglutinated only rabbit erythrocytes
and was inhibited by mucin, asialomucin, asialofetuin and thyroglobulin. Lectin activity was stable up to 80°C and under wide
range of pH (2.0–9.3). SDS-PAGE and gel filtration results showed the lectin is a homotetramer of Mr 49.5 kDa, but MALDI analysis
showed two distinct peaks corresponding to subunit mass of 12 kDa and 12.7 kDa. Also the N-terminal sequencing gave two different
sequences indicating presence of two polypeptide chains. Cloning of RVL gene indicated posttranslational cleavage of RVL precursor
into two mature polypeptides of 116 and 117 amino-acid residues. Dynamic light scattering (DLS) and gel filtration studies
together confirmed the homogeneity of the purified lectin and supported RVL as a dimer with Mr 49.5 kDa derived from single
polypeptide precursor of 233 amino acids. Purified RVL exerts potent nematicidal activity on Meloidogyne incognita, a root knot nematode. Fluorescent confocal microscopic studies demonstrated the binding of RVL to specific regions of the
alimentary-tract and exhibited a potent toxic effect on M. incognita. RVL-mucin complex failed to interact with the gut confirming the receptor mediated lectin interaction. Very high mortality
(88%) rate was observed at lectin concentration as low as 30 μg/ml, suggesting its potential application in the development
of nematode resistant transgenic-crops. 相似文献
14.
Kawsar SM Fujii Y Matsumoto R Ichikawa T Tateno H Hirabayashi J Yasumitsu H Dogasaki C Hosono M Nitta K Hamako J Matsui T Ozeki Y 《Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology》2008,150(4):349-357
A lectin recognizing both Galbeta1-3GlcNAc and Galbeta1-4GlcNAc was purified from the demosponge Halichondria okadai by lactosyl-agarose affinity chromatography. The molecular mass of the lectin was determined to be 30 kDa by SDS-PAGE under reducing and non-reducing conditions and 60 kDa by gel permeation chromatography. The pI value of the lectin was 6.7. It was found to agglutinate trypsinized and glutaraldehyde-fixed rabbit and human erythrocytes in the presence and absence of divalent cations. The hemagglutinating activity by the lectin was inhibited by d-galactose, methyl-d-galactopyranoside, N-acetyl-d-galactosamine, methyl-N-acetyl-d-galactosaminide, lactose, melibiose, and asialofetuin. The K(d) of the lectin against p-nitrophenyl-beta-lactoside was determined to be 2.76x10(-5) M and its glycan-binding profile given by frontal affinity chromatography was shown to be similar to many other known galectins. Partial primary structure analysis of 7 peptides by cleavage with lysyl endopeptidase indicated that one of the peptides showed significant similarity with galectin purified from the sponge Geodia cydonium. 相似文献
15.
Background
Various proteins that display carbohydrate-binding activity in a Ca2+-dependent manner are classified into the C-type lectin family. They have one or two C-type carbohydrate-recognition domains (CRDs) composed of 110–130 amino acid residues in common. C-type lectins mediate cell adhesion, non-self recognition, and immuno-protection processes in immune responses and thus play significant roles in clearance of invaders, either as cell surface receptors for microbial carbohydrates or as soluble proteins existing in tissue fluids. The lectin of Spodoptera littoralis is still uncharacterized.Methodology
A single orf encoding a deduced polypeptide consisting of an 18-residue signal peptide and a 291-residue mature peptide, termed SpliLec, was isolated from the haemolymph of the cotton leafworm, S. littoralis, after bacterial challenge using RACE-PCR. Sequence analyses of the data revealed that SpliLec consists of two CRDs. Short-form CRD1 and long-form CRD2 are stabilized by two and three highly conserved disulfide bonds, respectively. SpliLec shares homology with some dipteran lectins suggesting possible common ancestor. The purified SpliLec exhibited a 140-kDa molecular mass with a subunit molecular mass of 35 kDa. The hemagglutination assays of the SpliLec confirmed a thermally stable, multisugar-binding C-type lectin that binds different erythrocytes. The purified SpliLec agglutinated microorganisms and exhibited comparable antimicrobial activity against gram (+) and gram (−) bacteria too.Conclusions
Our results suggested an important role of the SpliLec gene in cell adhesion and non-self recognition. It may cooperate with other AMPs in clearance of invaders of Spodoptera littoralis. 相似文献16.
A lectin from Zizyphus mauritiana lamk. has been purified from the 25–50% (NH4)2SO4 fraction of crude seed and cotyledonary leaf callus extracts. The lectins purified from the two sources had the same structure
and properties. Upon specific adsorption on Sephadex G-100, the lectin (ZML) could be displaced with 0.1 m d-glucose. ZML yielded a single band corresponding to a Mr of 66 kDa both in the absence and presence of β-mercaptoethanol on native- as well as in SDS-PAGE. It is thermostable but pH sensitive and agglutinates human erythrocytes
only. Lectin activity could also be detected in the cotyledons, leaf, and stem, and in their cultures, as well as in in vitro
regenerants. Cotyledons, cotyledonary leaf and its callus showed much higher lectin activity than seeds.
Received: 5 April 1997 / Revision received: 30 June 1997 / Accepted: 31 October 1997 相似文献
17.
Xiong‐Ya Wang Su‐Fen Bai Xin Li Xin‐Ming Yin Xian‐Chun Li 《Archives of insect biochemistry and physiology》2015,90(1):14-27
Although lysis of invading organisms is a major innate form of immunity used by invertebrates, it remains unclear whether herbivorous insects have hemolysin or not. To address this general question, we tested the hemolytic (HL) activity of the hemolymph and tissue extracts from various stages of the polyphagous insect Helicoverpa armigera (Hübner) against the erythrocytes from chicken, duck, and rabbit. An HL activity was identified in the hemolymph of H. armigera larvae. Further studies demonstrated that the HL activity is proteinaceous as it was precipitable by deproteinizing agents. Hemolysins were found in Helicoverpa egg, larva, pupa, and adult, but the activity was higher in feeding larvae than in molting or newly molted larvae. Hemolysins were distributed among a variety of larval tissues including salivary gland, fat body, epidermis, midgut, or testes, but the highest activity was found in salivary gland and fat body. Relative to nonparasitized larvae, parasitization of H. armigera larvae by the endoparasitoid Campoletis chlorideae Uchida induced a 3.4‐fold increase in the HL activity in the plasma of parasitized host at day two postparasitization. The present study shows the presence of a parasitoid inducible HL factor in the parasitized insect. The HL activity increased significantly in H. armigera larvae at 12 and 24 h postinjection with Escherichia coli. We infer the HL factor(s) is inducible or due to de novo synthesis, which means that the HL factor(s) is associated with insect immune response by inhibiting or clearance of invading organisms. 相似文献
18.
Ganesh Arumugam Hilda Karuppiah Bhuvaragavan Sreeramulu Ramaraj Paulchamy Janarthanan Sundaram 《Entomological Science》2019,22(3):239-249
Insects depend on lectins for non‐self recognition and clearance of invading pathogens. Naturally occurring lectin showing specificity for galactose was purified from the serum of lepidopteran pest Parasa lepida by affinity chromatography using Sepharose 6B coupled with galactose as a gel matrix. Preliminary studies on crude serum agglutinin revealed that the agglutinin molecule showed varying degrees of specificity to avian and mammalian red blood cells tested. Among them, the highest titer of 128 was recorded against rabbit red blood cell type. The agglutinin molecule in the crude serum was stable up to 60°C and at pH between 6 and 9. Also, the hemagglutinating activity was neither dependent on divalent cations nor sensitive to ethylenediaminetetraacetic acid treatment. Galactose inhibited the hemagglutinating activity at minimum inhibitory concentration of 12.5 mM and hence it was used as a ligand for affinity chromatography. Native polyacrylamide gel electrophoresis analysis revealed a single band and the molecular weight of the lectin was found to be approximately 90 kDa. Bacterial agglutination activity of the purified lectin with two significant toxin bacteria, namely Salmonella typhi and Bacillus thuringiensis, was observed. 相似文献
19.
Chrysomya albiceps and Chrysomya megacephala are exotic blowfly species known by producing myiasis in humans and other animals and by transmitting pathogens mechanically. C. albiceps stand out by being a facultative predator of other dipteran larvae. In this paper we investigated the influence of larval predation on the dispersal of larvae of C. albiceps and C. megacephala single and double species for three photophases. An experimental acrylic channel graduated and covered with wood shavings was used to observe the larval dispersal. The results showed that C. albiceps attacks C. megacephala larvae during dispersal and keeps an aggregated pattern close to the release point, in single and double species, independently of the different photophases. Chrysomya megacephala single species exhibited the same pattern, but in double species this was changed to a random distribution. 相似文献
20.
《Bioscience, biotechnology, and biochemistry》2013,77(8):1237-1242
A lectin was isolated from hemolymph of the Southeast Asian horseshoe crab Tachypleus gigas by using glycophorin HA affinity chromatography and Sephacryl S-300 gel filtration. The purified lectin had a molecular mass of approximately 396 kDa and was composed of 13 identical subunits with molecular masses of 31 kDa. The serological specificity of the purified lectin was specifically inhibited by sialic acids sialoglycoproteins, but not by neutral sugars, hexosamines, N-acetylhexosamines, or asialoglycoproteins. Although the N-terminal amino acid sequence of the lectin from T. gigas was identical to that from American horseshoe crab (liphemin) by the same purification method and cross reacted with the anti-liphemin serum, the calcium concentration of hemagglutinating activity of the purified lectin showed a smaller optimal concentration than that of liphemin. 相似文献