JPH07238097A - Igg antibody comprising inhibin as antigen - Google Patents
Igg antibody comprising inhibin as antigenInfo
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- JPH07238097A JPH07238097A JP23863394A JP23863394A JPH07238097A JP H07238097 A JPH07238097 A JP H07238097A JP 23863394 A JP23863394 A JP 23863394A JP 23863394 A JP23863394 A JP 23863394A JP H07238097 A JPH07238097 A JP H07238097A
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Abstract
Description
【0001】[0001]
【産業上の利用分野】この発明は、インヒビン(INH
IBIN)の抗体に関する。インヒビンは、避妊薬とし
てあるいは畜産に利用できる性ホルモンであり、その抗
体は不妊症等の診断薬として利用できる。BACKGROUND OF THE INVENTION The present invention relates to inhibin (INH
IBIN) antibody. Inhibin is a sex hormone that can be used as a contraceptive or for livestock production, and its antibody can be used as a diagnostic agent for infertility and the like.
【0002】[0002]
【従来の技術】インヒビンは、Mc Cullagh (Science, 7
6, 19-20,(1932))により去勢動物の下垂体に見られる去
勢細胞の出現を抑制する精巣の水溶性の抽出物として見
い出された。卵巣性インヒビンとしては、De Jong ら(N
ature, 263, 71-72,(1976)) によりウシの卵胞液中に見
い出され、その後、ラット,ブタ,サル,ヒツジ,ウ
マ,ヒトなどの卵胞液中に多量のインヒビン活性が存在
することが確かめられている。現在では、インヒビンは
雌雄両性の性腺に存在する水溶性の物質で、下垂体から
のFSH(卵胞刺激ホルモン)の合成,分泌を特異的に
抑制する物質として考えられている。インヒビンは卵胞
の発育,成熟,***などの現象にも関与していて視床下
部下垂体性腺系で生殖生理上、重要な役割を果してい
る。2. Description of the Related Art Inhibin is Mc Cullagh (Science, 7
6, 19-20, (1932)), which was found as a water-soluble extract of testis that suppresses the appearance of castration cells found in the pituitary gland of castrated animals. As ovarian inhibin, De Jong et al.
ature, 263 , 71-72, (1976)) found in bovine follicular fluid, and then a large amount of inhibin activity was present in follicular fluid of rats, pigs, monkeys, sheep, horses, humans, etc. It has been confirmed. Currently, inhibin is a water-soluble substance present in both sexes of the sexes, and is considered to be a substance that specifically inhibits the synthesis and secretion of FSH (follicle-stimulating hormone) from the pituitary gland. Inhibin is also involved in phenomena such as follicle development, maturation, and ovulation, and plays an important role in reproductive physiology in the hypothalamic pituitary gland system.
【0003】卵巣性インヒビンの内、ブタのものについ
て Williamら(Partial Purification of Porcine Follc
ular Fluid Gonadostatin, Intraovarian Control Mech
anisms, Advances Experimental Medicine and Biolog
y, vol.147, Plenum Press, New York, 99-116, 1982)
はブタ卵胞液の「セファクリルS−300」によるゲル
濾過クロマトグラフィーの溶出液中分子量26,000
の画分にインヒビン活性があることを見い出している。
しかるに、この文献においては、インヒビンは精製され
ておらず、従って、インヒビン活性は単一の物質によっ
て発現されるのか、あるいはインヒビン活性を有する複
数の物質が存在するのかは明らかにされていない。現に
我々の研究によれば、ブタ卵胞液中には分子量3万近辺
のものに限っても、少くとも3種のインヒビン活性を有
する物質が見い出されている。Among the ovarian inhibins, the pig one was described by William et al. (Partial Purification of Porcine Follc
ular Fluid Gonadostatin, Intraovarian Control Mech
anisms, Advances Experimental Medicine and Biolog
y, vol.147, Plenum Press, New York, 99-116, 1982)
Is a molecular weight 26,000 in the eluate of gel filtration chromatography with "Sephacryl S-300" of porcine follicular fluid.
It has been found that the fractions of E. coli have inhibin activity.
However, in this document, inhibin has not been purified, and therefore it is not clarified whether inhibin activity is expressed by a single substance or whether there are multiple substances having inhibin activity. In fact, according to our research, at least three kinds of substances having inhibin activity have been found in porcine follicular fluid, even if it has a molecular weight of around 30,000.
【0004】[0004]
【発明が解決しようとする課題】叙上のように、従来イ
ンヒビンは単一の物としては分離されていないため、そ
の特異な生理活性からして避妊薬等に使用できる大きな
可能性があるにも拘らず、その応用はできなかった。従
って、この発明の目的はインヒビンを単一の物質として
得、単一の物質として得られたインヒビンを抗原とする
抗体を得ることにある。As described above, since inhibin has not been isolated as a single substance in the past, it has a great potential to be used as a contraceptive due to its unique physiological activity. Nevertheless, it could not be applied. Therefore, an object of the present invention is to obtain inhibin as a single substance and to obtain an antibody whose antigen is the inhibin obtained as a single substance.
【0005】[0005]
【課題を解決するための手段】本発明者らは、ブタの卵
胞液よりインヒビンを単一物質として分離,精製し、そ
の物理的,化学的性質を明らかにすることに成功した。
更に、得られた卵巣性インヒビンを抗原とするIgG抗
体を得ることに成功した。The present inventors have succeeded in separating and purifying inhibin as a single substance from porcine follicular fluid and clarifying its physical and chemical properties.
Furthermore, we succeeded in obtaining an IgG antibody using the obtained ovarian inhibin as an antigen.
【0006】すなわち、本発明は以下の性質を有するイ
ンヒビンを抗原とするIgG抗体に関する。 (a)分子量:32kd(SDS−ゲル電気泳動法及び
高速液体クロマトグラフィー法) (b)還元により分子量20kdと13kd(SDS−
ゲル電気泳動法)のポリペプチドが生じ、活性を失う。 (c)コンカナバリンAセファロースカラムに吸着さ
れ、α−メチルマンノシドによって溶出される。 (d)等電点:pI6付近 (e)プロテアーゼ処理により失活し、ノイラミニダー
ゼ処理及びエンドグリコシダーゼH処理により失活しな
い。 (f)N−末端アミノ酸配列: 分子量20×103 のポリペプチド:Ser Thr Ala Pro 分子量13×103 のポリペプチド:Gly Leu Glu Cys (g)ブタ卵胞液中に存在し、卵胞刺激ホルモンの上昇
を抑制する。That is, the present invention relates to an IgG antibody using inhibin as an antigen having the following properties. (A) Molecular weight: 32 kd (SDS-gel electrophoresis method and high performance liquid chromatography method) (b) Molecular weight 20 kd and 13 kd (SDS- by reduction)
Gel electrophoresis) polypeptide occurs and loses its activity. (C) Adsorbed on a concanavalin A sepharose column and eluted with α-methyl mannoside. (D) Isoelectric point: around pI6 (e) Inactivated by protease treatment, but not by neuraminidase treatment and endoglycosidase H treatment. (F) N-terminal amino acid sequence: Polypeptide having a molecular weight of 20 × 10 3 : Ser Thr Ala Pro Polypeptide having a molecular weight of 13 × 10 3 : Gly Leu Glu Cys (g) Exists in the follicular fluid of pigs and Suppress the rise.
【0007】上記のインヒビンは、例えば以下の方法で
得ることができる。ブタ卵巣を集め、卵胞液を吸引等に
より採取する。インヒビンは、「マトリックス ゲル
レッドA」(アミコン社)に特異的に吸着されるので
(Molecularand Cellular Endocrinology, 21, 109-11
7,(1981)) 、まず、このゲルによるアフィニティークロ
マトグラフィーを行う。次いで、本発明者らの研究によ
れば、「フェニルセファロース」,「セファクリル S
−200」,「DEAE セファクリル CL6B」に
よるクロマトグラフィー及び最後に逆相高速液体クロマ
トグラフィーによる精製がこの物質の精製には最も適し
ている。これらのクロマトグラフィーにおける溶離溶媒
としては8Mウレアが最適である。The above-mentioned inhibin can be obtained, for example, by the following method. Collect pig ovaries and collect follicular fluid by suction or the like. Inhibin is a “matrix gel
It is specifically adsorbed by "Red A" (Amicon) (Molecular and Cellular Endocrinology, 21 , 109-11
7, (1981)), first, affinity chromatography using this gel is performed. Next, according to the research conducted by the present inventors, "phenyl sepharose" and "sephacryl S"
Purification by chromatography on -200 "," DEAE Sephacryl CL6B "and finally by reversed phase high performance liquid chromatography is most suitable for purification of this material. 8M urea is the most suitable eluent in these chromatography.
【0008】このようにして精製されたインヒビンを抗
原として抗体を得る方法は、改訂5版細菌学実習提要,
医科学研究所学友会編,丸善株式会社,209頁,昭和
53年6月20日発行等に記載されている通常の方法で
よい。また、岩崎辰夫,安藤民衛,市川カオル,保井孝
太郎、単一クローン抗体,ハイブリドーマとELIS
A、講談社サイエンティフィック出版,第30頁,昭和
59年2月20日発行等に記載されている方法によりモ
ノクローナルとして得ることもできる。[0008] The method for obtaining an antibody using the thus purified inhibin as an antigen is described in the revised 5th edition Bacteriological Practice Guidelines,
The usual method described in the Institute of Medical Science, Alumni Association, Maruzen Co., Ltd., page 209, published June 20, 1978, etc. may be used. In addition, Tatsuo Iwasaki, Tamie Ando, Kaoru Ichikawa, Kotaro Yasui, Monoclonal antibody, hybridoma and ELIS
A can also be obtained as a monoclonal by the method described in Kodansha Scientific Publishing, page 30, published February 20, 1984, etc.
【0009】インヒビンの活性は、以下のようにして測
定することができる。 (1)ラット下垂体前葉細胞培養法 ラット下垂体前葉をトリプシン及びビオカーゼにより分
散し、細胞濃度5〜8万個/0.1ml/ウエルとなるよ
うにプラスチックプレートに入れる。各ウエルにインヒ
ビン検体0.1mlを加え、37℃に10%炭酸ガスを含
む空気中にて72時間保つ。培地はDMEMに5%ヒト
臍帯血清,2.5%FCS,5%馬血清を加えたものを用
いる。活性は培地中に放出されたFSH含量をラジオイ
ムノアッセイにより測定して、FSH放出の抑制度で以
って表わす。32Kインヒビン−IIは、ED50=1.2n
g/ml−培地の活性を持つ。The activity of inhibin can be measured as follows. (1) Rat anterior pituitary cell culture method The anterior pituitary of a rat is dispersed with trypsin and biocase, and placed in a plastic plate so that the cell concentration is 50,000 / 0.1 ml / well. 0.1 ml of inhibin sample was added to each well and kept at 37 ° C. for 72 hours in the air containing 10% carbon dioxide gas. The medium used is 5% human umbilical cord serum, 2.5% FCS, 5% horse serum added to DMEM. The activity is expressed by the degree of inhibition of FSH release measured by radioimmunoassay for the FSH content released in the medium. 32K inhibin-II has an ED 50 = 1.2n
g / ml-has the activity of medium.
【0010】(2)生体内試験法 35日令の雄ラットを去勢し、去勢後6から24時間に
かけて上昇してくる血中FSHをラジオイムノアッセイ
にて測定する。インヒビン検体は、去勢と同時に腹腔内
投与し、9時間後の血中FSH値の上昇に対する抑制程
度を測定する。この方法では(1)の方法に比べ約5,
000倍の検体量を必要とする。(2) In-vivo test method 35-day-old male rats are castrated, and blood FSH rising from 6 to 24 hours after castration is measured by radioimmunoassay. The inhibin sample is intraperitoneally administered at the same time as castration, and the degree of suppression of an increase in the blood FSH value after 9 hours is measured. This method requires about 5, compared to the method (1).
000 times the sample volume is required.
【0011】[0011]
【実施例】次に、本発明を実施例により詳しく説明す
る。 実施例1 (1)インヒビンの分離,精製 ブタ卵巣より吸引により卵細胞を採取し、10,000r
pm,1時間の遠心により上澄液を集めた。この上澄液
に2倍容の50mMトリス−塩酸緩衝液(pH7.5)を
加え、同じ緩衝液により緩衝化された「マトリックスゲ
ル レッドA」カラム(8.0×25cm)にのせ、次い
で上記緩衝液に0.15M KClを加えた溶液で充分洗
浄後、上記緩衝液に1.0M尿素と1.2M KClを加え
た溶液で溶出した。得られた溶出液に1/4容の2M
KClを加え、「フェニルセファロース」カラム(2.5
×30cm)にのせ、50mMトリス−塩酸緩衝液(p
H7.5)に1M KClを加えた緩衝液で充分洗浄後、
50mMトリス−塩酸緩衝液(pH7.5)に8M尿素を
加えた溶液で溶出した。EXAMPLES Next, the present invention will be described in detail with reference to Examples. Example 1 (1) Separation and Purification of Inhibin Egg cells were collected from pig ovary by suction to obtain 10,000 r
The supernatant was collected by centrifugation at pm for 1 hour. To this supernatant, 2 volumes of 50 mM Tris-hydrochloric acid buffer (pH 7.5) was added, and the mixture was placed on a “matrix gel red A” column (8.0 × 25 cm) buffered with the same buffer, and then the above-mentioned. After thorough washing with a solution containing 0.15 M KCl in the buffer, elution was performed with a solution containing 1.0 M urea and 1.2 M KCl in the above buffer. 1/4 volume of 2M in the obtained eluate
Add KCl and add “Phenyl Sepharose” column (2.5
X 30 cm) and 50 mM Tris-HCl buffer (p
After thoroughly washing with a buffer solution containing 1M KCl in H7.5),
Elution was performed with a solution of 8M urea added to a 50mM Tris-HCl buffer (pH 7.5).
【0012】溶出液を、「セファクリル S−200」
カラムを用いてゲル濾過クロマトグラフィーを行った。
展開緩衝液として8M尿素を含むトリス−塩酸緩衝液を
用いた。これにより分子量約8万と約3万の位置にイン
ヒビン活性が認められた。分子量3万の分画を集め、
「DEAE−セファロース CL6B」カラム(1.5×
30cm)を用いてイオン交換クロマトグラフィーを行
った。インヒビン活性は3個所に分れて溶出され、第二
のピークが最も活性が強かった(図1)。The eluate was "Sephacryl S-200".
Gel filtration chromatography was performed using the column.
A tris-hydrochloric acid buffer containing 8 M urea was used as a developing buffer. As a result, inhibin activity was recognized at positions of molecular weights of about 80,000 and about 30,000. Collecting fractions with a molecular weight of 30,000,
"DEAE-Sepharose CL6B" column (1.5 x
Ion exchange chromatography was carried out using 30 cm). The inhibin activity was separated and eluted in three places, and the second peak had the strongest activity (Fig. 1).
【0013】上記第二のピークの分画を集め、下記のよ
うに逆相高速液体クロマトグラフィーを行った。インヒ
ビン−IIはアセトニトリル濃度34%の位置に単一ピー
クとして溶出された。 カラム:「TSK−120T」,4.0×150mm, 溶出:(A)10%トリフルオル酢酸(TFA):アセ
トニトリル:水=1:10:90,(B)10%TF
A:アセトニトリル:水=1:60:40による直線グ
ラジェント。以上の精製工程における蛋白量,インヒビ
ン活性等の変化は第1表に示すとおりである。Fractions of the second peak were collected and subjected to reverse phase high performance liquid chromatography as described below. Inhibin-II was eluted as a single peak at the position where the concentration of acetonitrile was 34%. Column: “TSK-120T”, 4.0 × 150 mm, elution: (A) 10% trifluoroacetic acid (TFA): acetonitrile: water = 1: 10: 90, (B) 10% TF.
A: linear gradient with acetonitrile: water = 1: 60: 40. The changes in the amount of protein, inhibin activity and the like in the above purification steps are as shown in Table 1.
【0014】[0014]
【表1】 [Table 1]
【0015】得られた標品は、再逆相高速液体クロマト
グラフィー,SDS−ゲル電気泳動により単一であり、
そのインヒビン活性は卵胞液と比較して約5,000倍に
なっていた。卵細胞1リットルあたり約0.7mgの精製
標品が得られた。The obtained sample was single by re-reverse phase high performance liquid chromatography and SDS-gel electrophoresis,
Its inhibin activity was about 5,000 times that of follicular fluid. About 0.7 mg of purified preparation was obtained per liter of egg cell.
【0016】(2)32Kインヒビン−IIの物性 (a)逆相高速液体ゲル濾過クロマトグラフィー(カラ
ムTSK−3000SW)による分子量は32kdであ
る。 (b)SDS−ゲル電気泳動による分子量は、32kd
である。 (c)還元剤,酸化剤により容易に失活し、SDS−ゲ
ル電気泳動で分子量約20kdと約13kdの2つのポ
リペプチドが生じる。 (d)上記ポリペプチドのN−末端アミノ酸は、20k
dのものは Ser ThrAla Pro ,13kdのものは Gly
Leu Glu Cys であった。 (e)32Kインヒビン−IIは、コンカナバリンAセフ
ァロースカラムに吸着され、α−メチルマンノシドによ
って溶出されるので、糖蛋白質である。 (f)32Kインヒビン−IIは、プロテアーゼ処理によ
って失活する(トリプシンにて60%,ペプシンにて8
5%,キモトリプシンにて70%,プロナーゼにて95
%,サーモライシンにて98%失活する。)。 (g)32Kインヒビン−IIは、ノイラミニダーゼ処
理,エンドグリコシダーゼH処理によっては失活しな
い。 (h)等電点:pI6付近(2) Physical properties of 32K inhibin-II (a) The molecular weight by reverse phase high performance liquid gel filtration chromatography (column TSK-3000SW) is 32 kd. (B) The molecular weight by SDS-gel electrophoresis is 32 kd.
Is. (C) It is easily inactivated by a reducing agent and an oxidizing agent, and two polypeptides having a molecular weight of about 20 kd and about 13 kd are produced by SDS-gel electrophoresis. (D) The N-terminal amino acid of the above polypeptide is 20 k
Ser ThrAla Pro for d, Gly for 13kd
It was Leu Glu Cys. (E) 32K inhibin-II is a glycoprotein because it is adsorbed on the concanavalin A sepharose column and eluted with α-methylmannoside. (F) 32K inhibin-II is inactivated by protease treatment (trypsin 60%, pepsin 8
5%, 70% with chymotrypsin, 95 with pronase
%, Deactivate 98% with thermolysin. ). (G) 32K inhibin-II is not inactivated by treatment with neuraminidase and endoglycosidase H. (H) Isoelectric point: around pI6
【0017】(3)抗インヒビン抗体の調製 フロイントコンプリートアジュバンドと精製32Kイン
ヒビン−II(100μg/2ml)を等量混合し、日本
白色種家兎3羽の皮肉及び足蹠に与えた。2週間毎に上
記抗原を与え、3ヶ月後耳静脈より採血した。血清より
IgG画分を硫安沈澱により集めた。(3) Preparation of Anti-Inhibin Antibodies Freund's complete adjuvant and purified 32K inhibin-II (100 μg / 2 ml) were mixed in equal amounts and fed to the sarcasm and foot pads of 3 Japanese white rabbits. The above antigen was given every 2 weeks, and blood was collected from the ear vein after 3 months. The IgG fraction was collected from serum by ammonium sulfate precipitation.
【0018】[0018]
【発明の効果】本発明の抗インヒビン抗体は、インヒビ
ンの過少または過剰に起因する不妊症等の疾病の診断薬
として使用できる。INDUSTRIAL APPLICABILITY The anti-inhibin antibody of the present invention can be used as a diagnostic agent for diseases such as infertility caused by an inhibin insufficiency or excess.
【図1】 32Kインヒビン−IIのイオン交換クロマト
グラフィーの溶出パターンである。FIG. 1 is an elution pattern of 32K inhibin-II by ion exchange chromatography.
●─●:吸光度 ───:インヒビン活性 ───:NaCl濃度 ● ─ ●: Absorbance ───: Inhibin activity ───: NaCl concentration
───────────────────────────────────────────────────── フロントページの続き (72)発明者 長谷川 喜久 群馬県前橋市青柳町765の9 (72)発明者 寒川 賢治 宮崎県宮崎郡清武町加納甲1520−24 (72)発明者 松尾 寿之 宮崎県宮崎郡清武町木原6653A−104 (72)発明者 五十嵐 正雄 群馬県前橋市日吉町4丁目357−4 ─────────────────────────────────────────────────── ─── Continuation of front page (72) Inventor Yoshihisa Hasegawa 9 of 765 Aoyagi-cho, Maebashi City, Gunma Prefecture (72) Inventor Kenji Samukawa 1520-24 Kanoh, Kiyotake-cho, Miyazaki-gun, Miyazaki Prefecture (72) Toshiyuki Matsuo, Miyazaki Prefecture 6653 Kihara, Kiyotake-cho, Miyazaki-gun (72) Inventor Masao Igarashi 4-357-4 Hiyoshi-cho, Maebashi-shi, Gunma
Claims (1)
するIgG抗体。 (a)分子量:32kd(SDS−ゲル電気泳動法及び
高速液体クロマトグラフィー法) (b)還元により分子量20kdと13kd(SDS−
ゲル電気泳動法)のポリペプチドが生じ、活性を失う。 (c)コンカナバリンAセファロースカラムに吸着さ
れ、α−メチルマンノシドによって溶出される。 (d)等電点:pI6付近 (e)プロテアーゼ処理により失活し、ノイラミニダー
ゼ処理及びエンドグリコシダーゼH処理により失活しな
い。 (f)N−末端アミノ酸配列: 分子量20×103 のポリペプチド: Ser Thr Ala Pro 分子量13×103 のポリペプチド: Gly Leu Glu Cys (g)ブタ卵胞液中に存在し、卵胞刺激ホルモンの上昇
を抑制する。1. An IgG antibody using inhibin as an antigen, which has the following properties. (A) Molecular weight: 32 kd (SDS-gel electrophoresis method and high performance liquid chromatography method) (b) Molecular weight 20 kd and 13 kd (SDS- by reduction)
Gel electrophoresis) polypeptide occurs and loses its activity. (C) Adsorbed on a concanavalin A sepharose column and eluted with α-methyl mannoside. (D) Isoelectric point: around pI6 (e) Inactivated by protease treatment, but not by neuraminidase treatment and endoglycosidase H treatment. (F) N-terminal amino acid sequence: Polypeptide having a molecular weight of 20 × 10 3 Ser Ser Ala Pro Polypeptide having a molecular weight of 13 × 10 3 Gly Leu Glu Cys (g) Existence of follicle-stimulating hormone in porcine follicular fluid Suppress the rise.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
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JP23863394A JPH07238097A (en) | 1994-09-07 | 1994-09-07 | Igg antibody comprising inhibin as antigen |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP23863394A JPH07238097A (en) | 1994-09-07 | 1994-09-07 | Igg antibody comprising inhibin as antigen |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP60069209A Division JPH0730114B2 (en) | 1985-04-03 | 1985-04-03 | Inhibin |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH07238097A true JPH07238097A (en) | 1995-09-12 |
Family
ID=17033047
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP23863394A Pending JPH07238097A (en) | 1994-09-07 | 1994-09-07 | Igg antibody comprising inhibin as antigen |
Country Status (1)
Country | Link |
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JP (1) | JPH07238097A (en) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2015131254A1 (en) * | 2014-03-07 | 2015-09-11 | Ouro Fino Saúde Animal Ltda | Inhibin alpha antigen, gene coding for inhibin alpha, gene coding for fusion protein, method for obtaining inhibin alpha antigen, antigenic composition, use of the inhibin alpha antigen and use of the antigenic composition |
Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS63500309A (en) * | 1985-07-18 | 1988-02-04 | ザ・サルク・インステチユ−ト・フォ−・バイオロジカル・スタディ−ズ | Inhibin and its purification method |
-
1994
- 1994-09-07 JP JP23863394A patent/JPH07238097A/en active Pending
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS63500309A (en) * | 1985-07-18 | 1988-02-04 | ザ・サルク・インステチユ−ト・フォ−・バイオロジカル・スタディ−ズ | Inhibin and its purification method |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2015131254A1 (en) * | 2014-03-07 | 2015-09-11 | Ouro Fino Saúde Animal Ltda | Inhibin alpha antigen, gene coding for inhibin alpha, gene coding for fusion protein, method for obtaining inhibin alpha antigen, antigenic composition, use of the inhibin alpha antigen and use of the antigenic composition |
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