JPH05170800A - Lectin a obtained from tachypleus tridentatus or limuluspolyphemus and method for separating and purifying the same - Google Patents

Lectin a obtained from tachypleus tridentatus or limuluspolyphemus and method for separating and purifying the same

Info

Publication number
JPH05170800A
JPH05170800A JP34361891A JP34361891A JPH05170800A JP H05170800 A JPH05170800 A JP H05170800A JP 34361891 A JP34361891 A JP 34361891A JP 34361891 A JP34361891 A JP 34361891A JP H05170800 A JPH05170800 A JP H05170800A
Authority
JP
Japan
Prior art keywords
lectin
red blood
human
blood cells
horseshoe crab
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Pending
Application number
JP34361891A
Other languages
Japanese (ja)
Inventor
Masahito Matsukawa
雅仁 松川
Isami Tsuboi
五三美 坪井
Nobuyuki Sato
信行 佐藤
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Taiyo Fishery Co Ltd
Original Assignee
Taiyo Fishery Co Ltd
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Taiyo Fishery Co Ltd filed Critical Taiyo Fishery Co Ltd
Priority to JP34361891A priority Critical patent/JPH05170800A/en
Publication of JPH05170800A publication Critical patent/JPH05170800A/en
Pending legal-status Critical Current

Links

Landscapes

  • Peptides Or Proteins (AREA)

Abstract

PURPOSE:To obtain a new lectin A useful as a reagent for detecting complex carbohydrate containing a liberation type N-acetylamino sugar, a sialic acid such as N-acetylneuraminic acid and N-glycolylneuraminic acid and a bond type sialic acid in a test specimen of organism. CONSTITUTION:A lectin A obtained from blood lymph of Tachypleus tridentatus or Limuluspolyphemus, having affinity for N-acetylamino sugar, sialic acid, its complex carbohydrate and human and animal erythrocyte, showing the following properties. Emagglutination: showing agglutination reaction in the presence and absence of Ca<2+>. Human erythrocyte +++. Equine erythrocyte ++. Chicken erythrocyte +. The lectin A is produced from Tachypleus tridentatus or Limuluspolyphemus by using affinity chromatography.

Description

【発明の詳細な説明】Detailed Description of the Invention

【0001】[0001]

【産業上の利用分野】本発明は日本産カブトガニ (Tach
ypleus tridentatus) またはアメリカ産カブトガニ (Li
mulus polyphemus) の血リンパ液から得られる新しいレ
クチンAおよびその製造方法に関するものである。
The present invention relates to Japanese horseshoe crab (Tach
ypleus tridentatus) or American horseshoe crab (Li
The present invention relates to a new lectin A obtained from hemolymph fluid of (Mulus polyphemus) and a method for producing the same.

【0002】[0002]

【従来の技術】カブトガニは現在3属4種類が知られて
おり、そのうち、アメリカ産カブトガニ (Limulus poly
phemus) 、マルオカブトガニ (Carcinoscorpius rotund
icauda) 、日本産カブトガニ (Tachypleus tridentatu
s) の3種から赤血球凝集素 (レクチン) が分離されて
いる。
2. Description of the Related Art Horseshoe crab is currently known as four genera of three genera. Among them, the horseshoe crab (Limulus poly
phemus), Black-headed crab (Carcinoscorpius rotund)
icauda), Japanese horseshoe crab (Tachypleus tridentatu)
Hemagglutinin (lectin) has been isolated from the three species (s).

【0003】[0003]

【発明が解決しようとする課題】本発明の課題は、これ
ら従来のレクチンとは性質の異なる新規かつ有用なレク
チンを提供することにある。本発明者等は、日本産およ
びアメリカ産カブトガニの血リンパ液中に従来のレクチ
ンとは明らかに性質の異なるレクチンAの存在すること
を見いだし、これを分離しさらに部分精製することに成
功し、本発明を完成するに至ったものである。
An object of the present invention is to provide novel and useful lectins having properties different from those of the conventional lectins. The present inventors have found that lectin A, which is clearly different in property from conventional lectins, is present in the hemolymph of Japanese and American horseshoe crabs, and succeeded in separating and further partially purifying it. The invention has been completed.

【0004】[0004]

【課題を解決するための手段】本発明は、日本産カブト
ガニ (Tachypleus tridentatus) の血リンパ液より得ら
れ、N−アセチルアミノ糖、シアル酸およびその複合糖
質、ならびにヒトと動物の赤血球に親和性を有するレク
チンAであって、下記の性質を有するレクチンA 赤血球凝集性Ca2+の存在下、非存在下とも凝集反応を示
す。
The present invention is obtained from the hemolymph of Japanese horseshoe crab (Tachypleus tridentatus) and has an affinity for N-acetylamino sugar, sialic acid and its complex carbohydrate, and human and animal red blood cells. Which is a lectin A having the following properties and shows an agglutination reaction in the presence and absence of hemagglutinating Ca 2+ .

【0005】ヒト赤血球 +++ ウマ赤血球 ++ ニワトリ赤血球 + ならびにアメリカ産カブトガニ (Limulus polyphemus)
の血リンパ液より得られ、N−アセチルアミノ糖、シア
ル酸およびその複合糖質、ならびにヒトと動物の赤血球
に親和性を有するレクチンAであって、下記の性質を有
するレクチンA赤血球凝集性Ca2+の存在下、非存在下と
も凝集反応を示す。
Human red blood cells +++ Horse red blood cells ++ Chicken red blood cells + and American horseshoe crab (Limulus polyphemus)
Lectin A, which is obtained from the hemolymph fluid of Escherichia coli and has an affinity for N-acetylamino sugar, sialic acid and its complex carbohydrate, and human and animal red blood cells, and has the following properties: Lectin A hemagglutinating Ca 2 Aggregation reaction is shown both in the presence and absence of + .

【0006】ヒト赤血球 +++ ウマ赤血球 ++ ニワトリ赤血球 + を提供することを目的とする。さらに、本発明は、シア
ロ糖タンパク質を固定リガンドとするアフィニティーク
ロマトグラフィーと、ゲル濾過法とを用いて、日本産カ
ブトガニ (Tachypleustridentatus) またはアメリカ産
カブトガニ (Limulus polyphemus) の血リンパ液から前
記本発明のレクチンAを取得することを特徴とするレク
チンAの製造方法を提供することを目的とする。
[0006] Human red blood cells +++ Horse red blood cells ++ It is aimed to provide chicken red blood cells +. Furthermore, the present invention uses the affinity chromatography using a sialoglycoprotein as a fixed ligand and a gel filtration method to extract the lectin of the present invention from the hemolymph of Japanese horseshoe crab (Tachypleus tridententatus) or American horseshoe crab (Limulus polyphemus). It is an object of the present invention to provide a method for producing lectin A characterized in that A is obtained.

【0007】以下、本発明を詳細に説明する。本発明の
レクチンAは、例えば、日本産またはアメリカ産カブト
ガニの血リンパ液よりヒト赤血球膜シアロ糖タンパク質
を固定リガンドとするアフィニティークロマトグラフィ
ーにより分離され、さらにセファクリルを支持体とする
ゲル濾過を併用することによって部分精製される。ゲル
濾過の溶出液としては、好ましくはチオシアン酸カリウ
ムを含むトリス−塩酸緩衝液が挙げられる。
The present invention will be described in detail below. The lectin A of the present invention is, for example, separated from the hemolymph of Japanese or American horseshoe crab by affinity chromatography using a human erythrocyte membrane sialoglycoprotein as a fixed ligand, and further combined with gel filtration using sephacryl as a support. Partially purified by. As the eluate for gel filtration, a tris-hydrochloric acid buffer containing potassium thiocyanate is preferably used.

【0008】ヒト赤血球膜シアロ糖タンパク質をリガン
ドとした場合、次の性質を持つレクチンが単離される。 N−アセチルアミノ糖 + N−アセチルノイラミン酸 ++ N−グライコリルノイラミン酸 + なお、本発明レクチンAは上記糖鎖との結合反応やヒト
および動物の赤血球の凝集反応に際し、Ca2+イオンを必
要とせず、同種及び他種のカブトガニより得られている
既知のレクチンはいずれもCa2+イオンを必要とする点に
おいて明らかに異なっている。
When human red blood cell membrane sialoglycoprotein is used as a ligand, a lectin having the following properties is isolated. N-acetylamino sugar + N-acetylneuraminic acid ++ N-glycolylneuraminic acid + In addition, the lectin A of the present invention causes Ca 2+ in the binding reaction with the sugar chain and the agglutination reaction of human and animal red blood cells. The known lectins obtained from the same species and other species of horseshoe crab, which do not require ions, clearly differ in that they require Ca 2+ ions.

【0009】[0009]

【実施例】次に実施例を挙げて本発明を説明する。 〔実施例1〕(1) Lis −フェノール抽出法 (V.T. Marc
hesi and E.P. Andrews,174, 1247(1971) によりヒトの
赤血球膜から得られたシアロ糖タンパク質 (グリコホリ
ンHA) 50mgをアフィゲル10 (バイオラッドラボラトリー
ズ社製) 25mlに結合させてアフィニティークロマトグラ
フィー用支持体を作製した。この支持体を用いたカラム
を1.0M KSCNと0.3M NaClを含む 50mM トリス−塩酸緩
衝液 (以下「Tris-HCl」という) (pH7.2) で洗浄し、 1
0mM CaCl2 と0.3M NaClを含む50mM Tris-HCl (pH7.2)
で十分平衡化した後、カラムに日本産またはアメリカ産
カブトガニの血リンパ液 (10〜50ml) を加えた。カラム
から非吸着物質を同緩衝液を用いて流出させた後、カラ
ムから吸着物質を2〜10mM EDTA を含む、0.3M NaCl、
50mMTris-HCl (pH7.2)で溶出してCaイオン依存性の吸着
画分を得た。次に、0.5M チオシアン酸カリウム (KSC
N) を含む、0.3M NaCl、50mM Tris-HCl (pH7.2) で目
的の吸着物質を溶出した (以下「KSCN画分」という (図
1参照))。
EXAMPLES Next, the present invention will be described with reference to examples. [Example 1] (1) Lis-phenol extraction method (VT Marc
50 mg of sialoglycoprotein (glycophorin HA) obtained from human erythrocyte membrane by hesi and EP Andrews, 174 , 1247 (1971) was bound to 25 ml of Affigel 10 (Bio-Rad Laboratories) to obtain a support for affinity chromatography. It was made. The column using this support was washed with 50 mM Tris-HCl buffer (hereinafter referred to as “Tris-HCl”) (pH 7.2) containing 1.0 M KSCN and 0.3 M NaCl, and 1
50 mM Tris-HCl (pH 7.2) containing 0 mM CaCl 2 and 0.3 M NaCl
After sufficiently equilibrating with, hemolymph fluid (10 to 50 ml) of Japanese or American horseshoe crab was added to the column. After the non-adsorbed substance was made to flow out from the column using the same buffer solution, the adsorbed substance was extracted from the column with 2 to 10 mM EDTA, 0.3 M NaCl,
It was eluted with 50 mM Tris-HCl (pH 7.2) to obtain a Ca ion-dependent adsorption fraction. Next, 0.5M potassium thiocyanate (KSC
The target adsorbed substance was eluted with 0.3 M NaCl, 50 mM Tris-HCl (pH 7.2) containing N) (hereinafter referred to as “KSCN fraction” (see FIG. 1)).

【0010】このKSCN画分を分子篩膜(PM-30, 分画分子
量:30,000) を用いて濃縮した後、この濃縮液をあらか
じめ0.5M KSCNを含む0.3M NaCl、50mM Tris-HCl (pH
7.2)緩衝液で平衡化したセファクリル S-300 (ファルマ
シア社製) カラム (1.0×70cm) に添加した。同緩衝液
を用いて溶出し、ヒト赤血球に対し凝集活性を示す画分
を集めて本発明のレクチンAを得た (図2参照) 。
The KSCN fraction was concentrated using a molecular sieve membrane (PM-30, molecular weight cut off: 30,000), and the concentrated solution was preliminarily diluted with 0.5 M KSCN in 0.3 M NaCl and 50 mM Tris-HCl (pH).
7.2) It was added to a Sephacryl S-300 (Pharmacia) column (1.0 × 70 cm) equilibrated with a buffer solution. Elution was performed using the same buffer solution, and the fractions showing agglutinating activity on human erythrocytes were collected to obtain lectin A of the present invention (see FIG. 2).

【0011】(2) 本発明のレクチンAの分子量は、0.5
M KSCNを含む0.3M NaCl、50mM Tris-HCl (pH7.2) 緩衝
液で平衡化したセファクリル S-300を支持体とするゲル
濾過法から概算するといずれも約170万であり、日本産
やアメリカ産、および東南アジア産カブトガニレクチン
B、さらに既知レクチンの分子量とは明らかに異なって
いる (図3) 。
(2) The lectin A of the present invention has a molecular weight of 0.5.
Estimated by gel filtration method using Sephacryl S-300 equilibrated with 0.3 M NaCl, 50 mM Tris-HCl (pH7.2) buffer containing M KSCN, the total was about 1.7 million. The molecular weights of horseshoe crab lectin B produced in Southeast Asia and known lectin are clearly different (Fig. 3).

【0012】(3) 本発明の両レクチンAは、グルコー
ス、マンノース、ガラクトース、フコース等の中性糖、
グルコサミン、ガラクトサミン等のアミノ糖とは反応し
なかったが、N−アセチルグルコサミン、N−アセチル
ガラクトサミン等のN−アセチルアミノ糖、N−アセチ
ルノイラミン酸、N−グライコリルノイラミン酸、ウシ
の顎下腺ムチン、フェツイン等とは反応した (表1) 。
表1は、ヒト赤血球に対して23 の凝集活性を有するレ
クチンAを用いたときの結果を示す。
(3) Both lectins A of the present invention are neutral sugars such as glucose, mannose, galactose and fucose,
It did not react with amino sugars such as glucosamine and galactosamine, but N-acetylglucosamine, N-acetylamino sugars such as N-acetylgalactosamine, N-acetylneuraminic acid, N-glycolylneuraminic acid, and bovine jaw It reacted with mucins of the lower gland, fetuin, etc. (Table 1).
Table 1 shows the results when using lectin A having an agglutinating activity of 2 3 on human erythrocytes.

【0013】(4) 本発明の両レクチンAは、ウマ赤血
球よりもヒト赤血球を著しく強く凝集し、さらに凝集反
応にはCa+3イオンを必要としない性質を有するものであ
り、日本産やアメリカ産、および東南アジア産カブトガ
ニレクチンB、さらに既知レクチンが凝集反応にCa2+
オンを必要とする点で明らかに相違している (表2) 。
表2において、凝集活性の測定は下記の条件で行った。 Ca2+非存在下 :0.3M KCl, 50mM Tris-HCl (pH7.2) Ca2+存在下 :0.3M KCl, 50mM Tris-HCl (pH7.2) 10mM CaCl2 以上、本発明の両レクチンAは市販レクチンや日本産カ
ブトガニより得られている既知レクチン (特開昭53-928
00号公報) 、さらにアメリカ産カブトガニレクチンB
(特願平3-110631号) や日本産カブトガニレクチンB
(特願平3-246463号) 、さらに東南アジア産カブトガニ
レクチンB (特願平3-280813号) とも明らかに相違し、
糖鎖との反応や赤血球凝集反応に対しCa2+イオンを必要
としない性質を有し、遊離型と結合型のシアル酸および
N−アセチルアミノ糖に対し結合性を有する新規レクチ
ンである。
(4) Both lectins A of the present invention remarkably agglutinate human erythrocytes more strongly than equine erythrocytes and do not require Ca +3 ion for agglutination reaction. There is a clear difference in that the horseshoe crab lectin B produced in Southeast Asia and the known lectin require Ca 2+ ions for the agglutination reaction (Table 2).
In Table 2, the aggregation activity was measured under the following conditions. In the absence of Ca 2+ : 0.3M KCl, 50mM Tris-HCl (pH7.2) In the presence of Ca 2+ : 0.3M KCl, 50mM Tris-HCl (pH7.2) 10mM CaCl 2 or more, both of the present invention Lectin A is a commercially available lectin or a known lectin obtained from Japanese horseshoe crab (JP-A-53-928).
No. 00), and further American horseshoe crab lectin B
(Japanese Patent Application No.3-110631) and Japanese horseshoe crab lectin B
(Japanese Patent Application No. 3-246463) and the horseshoe crab lectin B from Southeast Asia (Japanese Patent Application No. 3-280813) are also clearly different.
It is a novel lectin having the property of not requiring Ca 2+ ions for the reaction with sugar chains and hemagglutination reaction and having the binding properties to free and bound sialic acid and N-acetylamino sugar.

【0014】[0014]

【表1】 [Table 1]

【0015】[0015]

【表2】 [Table 2]

【0016】[0016]

【発明の効果】本発明のレクチンAは新規なものであ
り、生物試料中の遊離型のN−アセチルアミノ糖、およ
びN−アセチルノイラミン酸やN−グライコリルノイラ
ミン酸のようなシアル酸および結合型シアル酸を持つ複
合糖質を検出するための試薬として有用である。また、
結合型シアル酸を持つ複合糖質には、生理活性物質が数
多く知られており、本発明のレクチンAはそれらの分離
精製用、アフィニティークロマトグラフィーの吸着担体
としても有効である。
INDUSTRIAL APPLICABILITY The lectin A of the present invention is novel, and is free of N-acetylamino sugars in biological samples and sialic acids such as N-acetylneuraminic acid and N-glycolylneuraminic acid. It is also useful as a reagent for detecting glycoconjugates having bound sialic acid. Also,
A large number of physiologically active substances are known for glycoconjugates having bound sialic acid, and the lectin A of the present invention is also effective as an adsorption carrier for their separation and purification and affinity chromatography.

【0017】なお、一般に動物由来のレクチンはその作
用発現においてCa2+イオンなどの金属イオンを必要とす
るが、本発明のレクチンAはCa2+イオンを必要としない
事実は、動物レクチンの分子機構の解明において極めて
重要な性質を有するものである。
In general, animal-derived lectins require metal ions such as Ca 2+ ions for their action expression, but the fact that the lectin A of the present invention does not require Ca 2+ ions means that animal lectin molecules It has a very important property in elucidating the mechanism.

【図面の簡単な説明】[Brief description of drawings]

【図1】ヒト赤血球膜シアロ糖タンパク質を固定リガン
ドとするアフィニティークロマトグラフィー溶出画分の
凝集活性を示す〔ヒト赤血球 (Ca2+非存在下) における
凝集活性〕。 A:0.5M KSCN, 0.3M NaCl, 50mM Tris-HCl (pH7.2)
FIG. 1 shows the agglutination activity of an affinity chromatography elution fraction using human erythrocyte membrane sialoglycoprotein as a fixed ligand [agglutination activity in human erythrocytes (in the absence of Ca 2+ )]. A: 0.5M KSCN, 0.3M NaCl, 50mM Tris-HCl (pH7.2)

【図2】セファクリル S-300を支持体とするゲル濾過溶
出画分の凝集活性を示す〔ヒト赤血球 (Ca2+非存在下)
における凝集活性〕。 V。:ボイド・ボリューム (void volume)
FIG. 2 shows the agglutination activity of gel filtration elution fractions using Sephacryl S-300 as a support [human erythrocytes (in the absence of Ca 2+ ).
Aggregating activity in]. V. : Void volume

【図3】ゲル濾過法から概算される分子量を示す。FIG. 3 shows the estimated molecular weight from the gel filtration method.

Claims (4)

【特許請求の範囲】[Claims] 【請求項1】 日本産カブトガニ (Tachypleus trident
atus) の血リンパ液より得られ、N−アセチルアミノ
糖、シアル酸およびその複合糖質、ならびにヒトと動物
の赤血球に親和性を有するレクチンAであって、下記の
性質を有するレクチンA。赤血球凝集性Ca2+の存在下、
非存在下とも凝集反応を示す。 ヒト赤血球 +++ ウマ赤血球 ++ ニワトリ赤血球 +
1. A Japanese horseshoe crab (Tachypleus trident)
Lactin A having affinities for N-acetylamino sugar, sialic acid and its complex carbohydrate, and human and animal erythrocytes, which are obtained from the hemolymph of Atus). In the presence of hemagglutinating Ca 2+ ,
Aggregation reaction is shown even in the absence. Human red blood cells +++ Horse red blood cells ++ Chicken red blood cells +
【請求項2】 アメリカ産カブトガニ (Limulus polyph
emus) の血リンパ液より得られ、N−アセチルアミノ
糖、シアル酸およびその複合糖質、ならびにヒトと動物
の赤血球に親和性を有するレクチンAであって、下記の
性質を有するレクチンA。赤血球凝集性Ca2+の存在下、
非存在下とも凝集反応を示す。 ヒト赤血球 +++ ウマ赤血球 ++ ニワトリ赤血球 +
2. American horseshoe crab (Limulus polyph)
Lectin A having affinity for N-acetylamino sugar, sialic acid and its complex carbohydrate, and human and animal erythrocytes, which is obtained from the hemolymph fluid of E. In the presence of hemagglutinating Ca 2+ ,
Aggregation reaction is shown even in the absence. Human red blood cells +++ Horse red blood cells ++ Chicken red blood cells +
【請求項3】 シアロ糖タンパク質を固定リガンドとす
るアフィニティークロマトグラフィーと、ゲル濾過法と
を用いて、日本産カブトガニ (Tachypleus tridentatu
s) の血リンパ液から請求項1記載のレクチンAを取得
することを特徴とするレクチンAの製造方法。
3. Japanese horseshoe crab (Tachypleus tridentatu) using affinity chromatography using sialoglycoprotein as a fixed ligand and gel filtration.
A method for producing lectin A, wherein the lectin A according to claim 1 is obtained from the hemolymph fluid of s).
【請求項4】 シアロ糖タンパク質を固定リガンドとす
るアフィニティークロマトグラフィーと、ゲル濾過法と
を用いて、アメリカ産カブトガニ (Limuluspolyphemus)
の血リンパ液から請求項2記載のレクチンAを取得す
ることを特徴とするレクチンAの製造方法。
4. American horseshoe crab (Limulus polyphemus) using affinity chromatography using sialoglycoprotein as a fixed ligand and gel filtration method.
A method for producing lectin A, comprising obtaining the lectin A according to claim 2 from the hemolymph fluid of.
JP34361891A 1991-12-25 1991-12-25 Lectin a obtained from tachypleus tridentatus or limuluspolyphemus and method for separating and purifying the same Pending JPH05170800A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP34361891A JPH05170800A (en) 1991-12-25 1991-12-25 Lectin a obtained from tachypleus tridentatus or limuluspolyphemus and method for separating and purifying the same

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP34361891A JPH05170800A (en) 1991-12-25 1991-12-25 Lectin a obtained from tachypleus tridentatus or limuluspolyphemus and method for separating and purifying the same

Publications (1)

Publication Number Publication Date
JPH05170800A true JPH05170800A (en) 1993-07-09

Family

ID=18362928

Family Applications (1)

Application Number Title Priority Date Filing Date
JP34361891A Pending JPH05170800A (en) 1991-12-25 1991-12-25 Lectin a obtained from tachypleus tridentatus or limuluspolyphemus and method for separating and purifying the same

Country Status (1)

Country Link
JP (1) JPH05170800A (en)

Similar Documents

Publication Publication Date Title
US4269605A (en) Method and kit for separation of glycoproteins
Spiro [1] Analysis of sugars found in glycoproteins
Codington et al. Glycoprotein coat of the TA3 cell. Isolation and partial characterization of a sialic acid containing glycoprotein fraction
JP3537535B2 (en) Clinical test method based on immunoglobulin G-linked sugar chain structure
Gahmberg et al. Role of Sialic Acid in the Mobility of Membrane Proteins Containing O‐Linked Oligosaccharides on Polyacrylamide Gel Electrophoresis in Sodium Dodecyl Sulfate
Alborés et al. Purification and applications of a lectin from the mushroom Gymnopilus spectabilis
GB2024829A (en) Method and Product for Separation of Glycoproteins
El Rassi Recent developments in capillary electrophoresis of carbohydrate species
Gunnarsson et al. Oligosaccharide structures mediating agglutination of sheep erythrocytes by Staphylococcus saprophyticus
Cohen et al. [5] Purification of glycated hemoglobin
Muresan et al. Purification and use of limulin: a sialic acid-specific lectin.
AU2006257904B2 (en) Rapid saccharide biomarker assay
Mohan et al. Binding studies of a sialic acid-specific lectin from the horseshoe crab Carcinoscorpius rotunda cauda with various sialoglycoproteins
JPH05170800A (en) Lectin a obtained from tachypleus tridentatus or limuluspolyphemus and method for separating and purifying the same
Nordin et al. Structural and immunochemical studies on the phytotoxic peptidorhamnomannan of Ceratocystis ulmi
Shinozuka et al. Binding of lectins to “young” and “old” human erythrocytes
Gottlieb Polysaccharides of Crithidia fasciculata: identification and partial characterization of a cell surface constituent
JPH04338400A (en) Lectin b obtained from american horseshoe crab and method for separating and purifying the same lectin b
Law et al. Properties of lectins in the root and seed of Lotononis bainesii
JP5211311B2 (en) Novel lectin and method for producing the same, sugar chain detection method and sugar chain fractionation method
Lampio et al. Exposure of the major human red‐cell glycolipid, globoside, to galactose oxidase
JPH06263800A (en) Lectin b obtained from tachypleusgigas and its separation and purification
Pazur et al. Anti-glycosyl antibodies: antibodies directed against the carbohydrate moieties of a glycoprotein
US5523395A (en) Lectin species obtained from Japanese horseshoe crabs and from southern horseshoe crabs
Suganuma et al. Qualitative and quantitative analysis of erythrocyte surface membrane sialyl residues using affinity cytochemistry with special reference to diabetic patients