JPH0653760B2 - High molecular weight glycoprotein in milk - Google Patents
High molecular weight glycoprotein in milkInfo
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- JPH0653760B2 JPH0653760B2 JP18367085A JP18367085A JPH0653760B2 JP H0653760 B2 JPH0653760 B2 JP H0653760B2 JP 18367085 A JP18367085 A JP 18367085A JP 18367085 A JP18367085 A JP 18367085A JP H0653760 B2 JPH0653760 B2 JP H0653760B2
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- milk
- glycoprotein
- present
- molecular weight
- high molecular
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Description
【発明の詳細な説明】 産業上の利用分野 本発明は乳癌検診用の腫瘍マーカーとして有用な、霊長
類のミルク中に含まれる糖蛋白質に関する。TECHNICAL FIELD The present invention relates to a glycoprotein contained in primate milk, which is useful as a tumor marker for breast cancer screening.
従来の技術 ミルク中の成分に関する研究は、脂肪球膜（ＭＦＧＭ：
milk fat globule membrane）を用い盛んに行われてき
た。既に報告されている成分としてはHeid等による分子
量69000の糖蛋白質（Biochim．Biophys．Acta，728，22
8〜238，1983）や分子量155000，70000および39000のIm
amによる糖蛋白（Biochim．Ｊ．，193，47〜54，1981）
がある。また、清水，山内等は、これらとは違ったムチ
ン型の糖蛋白を見出し、ＰＡＳ−Ｏと命名した（Ｊ．Bi
ochim．，91，515〜524，1982）。2. Description of the Related Art Studies on ingredients in milk have been conducted on fat globule membrane (MFGM:
Milk fat globule membrane) has been actively used. As a component already reported, a glycoprotein having a molecular weight of 69000 (Biochim. Biophys. Acta, 728 , 22 by Heid et al.
8 ~ 238, 1983) and molecular weight 155,000, 70000 and 39000 Im
glycoprotein by am (Biochim. J., 193 , 47-54, 1981)
There is. Shimizu, Yamauchi et al. Found a mucin-type glycoprotein different from these and named it PAS-O (J. Bi.
ochim. , 91 , 515 to 524, 1982).
ＭＦＧＭ中のムチン型糖蛋白は、乳癌の研究の分野でも
研究されHilkens等によるMam６（Proc．Int．Workshop
on Monoclonal Antibodies and Breast Cancer，inpres
s）およびOrmerod等による上皮膜抗原（ＥＭＡ：epithe
lial membrane antigen）（Br．Ｊ．Cancer，48，533〜
541，1983）などが報告されているが、Mam６はその抗体
が前述のＰＡＳ−Ｏと反応すること、またＥＭＡもＰＡ
Ｓ−Ｏに由来する成分であることが、示唆され、ＰＡＳ
−Ｏとの差別化は困難である。また、ＰＡＳ−Ｏを含め
たこれらの成分が癌，特に乳癌患者の血中に存在するこ
とが確認されているが、いずれも癌のステージがかなり
進んだ状態でなければ検出できず、腫瘍マーカーとして
の実用性を有するものではなかった。The mucin-type glycoprotein in MFGM has been studied in the field of breast cancer research as well, and has been studied by Hilkens et al. In Mam6 (Proc. Int. Workshop).
on Monoclonal Antibodies and Breast Cancer, inpres
s) and Ormerod and other epithelial membrane antigens (EMA: epithe
lial membrane antigen) (Br. J. Cancer, 48 , 533-
541, 1983) and the like, but Mam6 shows that the antibody reacts with the above-mentioned PAS-O.
It has been suggested that it is a component derived from S-O.
-It is difficult to differentiate from O. Further, it has been confirmed that these components including PAS-O are present in the blood of cancers, particularly breast cancer patients, but all of them can be detected only when the stage of cancer is considerably advanced, and they are tumor markers. However, it was not practical.
発明が解決しようとする問題点 本発明者等はミルク特に霊長類のミルク中に含まれる糖
蛋白質について鋭意研究した結果、ＭＦＧＭおよび乳清
中に含まれ従来公知のものとは異なる新規な糖蛋白質を
見出しさらに研究を重ねて本発明を完成した。なお、本
発明の糖蛋白質は、初乳中に多く含まれるという利点を
有しており癌，特に乳癌患者の早期の段階で血中に出現
し、癌の早期発見のための腫瘍マーカーとして有用であ
る。DISCLOSURE OF THE INVENTION Problems to be Solved by the Invention As a result of diligent studies on the glycoprotein contained in milk, particularly primate milk, the present inventors have found that a novel glycoprotein contained in MFGM and whey and different from the conventionally known ones. The present invention was completed by further discovering the above. The glycoprotein of the present invention has the advantage that it is contained in a large amount in colostrum, and it appears in the blood at an early stage of cancer, especially in breast cancer patients, and is useful as a tumor marker for early detection of cancer. Is.
問題点を解決するための手段 本発明の糖蛋白質はウシのミルク中には存在しないが、
ヒトやサルのミルク中に存在した。Means for Solving the Problems Although the glycoprotein of the present invention is not present in bovine milk,
It was found in human and monkey milk.
本発明の糖蛋白質は、霊長類のミルク中のＭＦＧＭや乳
清より、常法により、例えばＭＦＧＭまたは乳清をゲル
ろ過することにより容易に得ることができる。本発明の
糖蛋白質の特性を以下に具体的に示す。The glycoprotein of the present invention can be easily obtained from MFGM or whey in primate milk by a conventional method, for example, by gel filtration of MFGM or whey. The characteristics of the glycoprotein of the present invention are specifically shown below.
１）ヒトおよびサル等の霊長類のＭＦＧＭや乳清中に存
在し、Sepharose（セファロース）ＣＬ−４Ｂカラム（P
harmacia社製）でゲルろ過するとき排除限界を越えた所
に流出し、またＳＤＳ−ＰＡＧＥ（sodium dodecyl sul
fateを含むポリアクリルアミドゲル電気泳動）の２％か
ら１０％のゲルグラディエントでは既存の糖蛋白質より
移動度の少ないバンドとして検出され、従来公知の成分
よりも更に高分子の糖蛋白質である。1) It exists in MFGM and whey of primates such as humans and monkeys, and Sepharose CL-4B column (P
When gel filtration is performed with harmacia), it flows out beyond the exclusion limit, and SDS-PAGE (sodium dodecyl sul)
In a gel gradient of 2% to 10% of polyacrylamide gel electrophoresis containing fate), it is detected as a band having less mobility than existing glycoproteins, and is a higher molecular glycoprotein than conventionally known components.
２）アミノ酸分析では、セリン，スレオニン含量がそれ
ぞれ総アミノ酸量に対し１０％を越える以外はすべて１
０％程度又は、１０％以下である。2) In the amino acid analysis, all were 1 except that the serine and threonine contents each exceeded 10% of the total amino acid content.
It is about 0% or 10% or less.
３）糖含量が全分子中の５０％以上を占める。3) The sugar content accounts for 50% or more of all molecules.
４）糖鎖構造はＰＮＡ（peanut agglutinin），ＷＧＡ
（wheat germ agglutinin）およびＳＢＡ（soybean agg
lutinin）などのレクチンと反応し、ConA（concanavali
nA）とは反応しない性質を有する。4) Sugar chain structure is PNA (peanut agglutinin), WGA
(Wheat germ agglutinin) and SBA (soybean agg
It reacts with lectins such as lutinin, and ConA (concanavali
It has the property of not reacting with nA).
実施例１ 乳清からの精製 人乳（出産後１週間以内のもの、および出産後１ヶ月以
上経過したもの）を１０００×ｇ，５℃で１０分間遠心
し、脱脂乳を得る。脱脂乳は室温にもどし、１Ｎ塩酸で
pH4.6に合わせて２時間放置する。次いで２５０００×
ｇで３０分間遠心し、カゼインを除去し乳清を得、透析
後凍結乾燥する。Example 1 Purified from whey Human milk (those within one week after delivery and one month or more after delivery) is centrifuged at 1000 × g at 5 ° C. for 10 minutes to obtain skim milk. Return skim milk to room temperature and add 1N hydrochloric acid.
Leave for 2 hours according to pH 4.6. Then 25000x
Centrifuge at g for 30 minutes to remove casein to obtain whey, dialysis and freeze-dry.
１００mgの乳清蛋白を１００ｍＭ塩化ナトリウムおよび
１０ｍＭデオキシコール酸ナトリウムを含むトリス−塩
酸バッファー（pH8.0）４mlに溶解し、同じバッファー
であらかじめ平衡化したセファロース（Sepharose）Ｃ
Ｌ−４Ｂ（（Pharmacia社製）カラム（1.5×６０cm）に
付し（４℃）分画した。本発明の化合物はカラムの排除
限界を越えて流出する第一分画（Ｆ1）に大部分回収さ
れ（第１図参照）、同一条件で再クロマトグラフィーに
より精製する。回収された第一分画は界面活性剤を除く
ためBio−beads SM2（Bio−Rad社製）カラムに付し
た。またサンプル中に混入する脂質を冷エタノール：エ
ーテル（１：１）で抽出除去し精製した。100 mg of whey protein was dissolved in 4 ml of Tris-hydrochloric acid buffer (pH 8.0) containing 100 mM sodium chloride and 10 mM sodium deoxycholate and pre-equilibrated with the same buffer, Sepharose C.
L-4B ((Pharmacia) column (1.5 × 60 cm) was applied and fractionated (4 ° C.). The compound of the present invention was found in the first fraction (F 1 ) flowing out beyond the exclusion limit of the column. Partially recovered (see Figure 1) and purified by re-chromatography under the same conditions The recovered first fraction was applied to a Bio-beads SM2 (Bio-Rad) column to remove the surfactant. Further, lipids mixed in the sample were extracted and removed with cold ethanol: ether (1: 1) for purification.
実施例２ ＭＦＧＭからの精製 実施例１で用いた人乳を３５℃で温めた後、２０００×
ｇで１０分間遠心し、生クリームを得る。生クリームは
３５℃で５倍量の１０ｍＭトリス−塩酸バッファー（pH
7.2）で３回洗浄し、クリームを得る。クリームは冷却
後、ポリトロン（キネマティカ社製）で激しく攪拌す
る。次いで４０℃で脂質微粒子を溶解後、遠心により水
層と脂質層に分離する。水層に２％（ｗ／ｗ）デオキシ
コール酸ナトリウム，８Ｍ尿素および１％（ｖ／ｖ）メ
ルカプトエタノールを加える。混合した水層は３７℃で
３０分間放置し、１５℃で１００００×ｇ，３０分間遠
心することにより澄明な水層を得る。この水層を実施例
１と同様にカラムクロマトグラフィーに付し、第一分画
に本発明の糖蛋白を得る。Example 2 Purification from MFGM After heating the human milk used in Example 1 at 35 ° C., 2000 ×
Centrifuge at g for 10 minutes to obtain a fresh cream. Fresh cream is 5 times volume of 10 mM Tris-HCl buffer (pH
Wash 3 times with 7.2) to obtain a cream. After cooling, the cream is vigorously stirred with Polytron (Kinematica). Next, after the lipid fine particles are dissolved at 40 ° C., they are separated into an aqueous layer and a lipid layer by centrifugation. To the aqueous layer is added 2% (w / w) sodium deoxycholate, 8M urea and 1% (v / v) mercaptoethanol. The mixed aqueous layer is left at 37 ° C. for 30 minutes and then centrifuged at 15 ° C. at 10,000 × g for 30 minutes to obtain a clear aqueous layer. This aqueous layer is subjected to column chromatography in the same manner as in Example 1 to obtain the glycoprotein of the present invention in the first fraction.
実施例１ ＳＤＳ ＰＡＧＥによる本発明の化合物の分析 ＳＤＳ ＰＡＧＥはWeberとOsbornの方法（Ｊ．Biol．C
hem．，244，4406〜4412，1969）を用い、アクリルアミ
ドゲルは２〜１０％のグラディエントゲルとした。サン
プルは初乳（出産後１週間以内のもの）および成熟乳
（出産後１ヶ月以上経過したもの）を各々、実施例１お
よび２に記載した方法により精製したものを用いた。泳
動されたバンドはＰＡＳ（periodic acid-Schiff）染色
を行った。その結果、本発明の糖蛋白質は、２％ゲルで
も殆ど移動されないところでＰＡＳ染色され、従来公知
のＰＡＳ−Ｏ等とは異なることおよび初乳中には多く存
在するが、成熟乳中には少ないことが明らかになった。Example 1 Analysis of Compounds of the Invention by SDS PAGE SDS PAGE was performed according to the method of Weber and Osborn (J. Biol. C.
hem. , 244 , 4406 to 4412, 1969), and the acrylamide gel was a 2 to 10% gradient gel. The samples used were colostrum (those within 1 week after delivery) and mature milk (those that passed 1 month after delivery) purified by the methods described in Examples 1 and 2, respectively. The electrophoresed band was stained with PAS (periodic acid-Schiff). As a result, the glycoprotein of the present invention is PAS-stained where it is hardly transferred even in 2% gel, is different from conventionally known PAS-O and the like, and is abundant in colostrum but is absent in mature milk. It became clear.
実施例２ アミノ酸分析による本発明の化合物の分析 実施例１および２で得られた本発明の糖蛋白質を日立８
３５アミノ酸分析装置により分析した。サンプルは真空
密封し、110℃で２４時間加水分解したものを用いた。
その結果を第２図に示す。図面中Ｂ，Ｔ，Ｚ，Ｐ，Ｇ，
Ａ，Ｃ，Ｖ，Ｍ，Ｉ，Ｌ，Ｙ，Ｆ，Ｋ，Ｈ，Ｒとあるの
はそれぞれアスパラギン酸＋アスパラギン，スレオニ
ン，セリン，グルタミン酸＋グルタミン，プロリン，グ
リシン，アラニン，システィン，バリン，メチオニン，
イソロイシン，ロイシン，チロシン，フェニール，アラ
ニン，リジン，ヒスチジン，アルギニンを表す。また図
面はアミノ酸全量に対する個々のアミノ酸の量を百分率
で示したものである。Example 2 Analysis of Compounds of the Present Invention by Amino Acid Analysis The glycoproteins of the present invention obtained in Examples 1 and 2 were analyzed by Hitachi 8
It was analyzed by a 35 amino acid analyzer. The sample was vacuum-sealed and hydrolyzed at 110 ° C. for 24 hours.
The results are shown in FIG. B, T, Z, P, G, in the drawing
A, C, V, M, I, L, Y, F, K, H, R are aspartic acid + asparagine, threonine, serine, glutamic acid + glutamine, proline, glycine, alanine, cystine, valine, methionine, respectively. ，
Represents isoleucine, leucine, tyrosine, phenyl, alanine, lysine, histidine, arginine. The drawing also shows the amount of each amino acid as a percentage of the total amount of amino acids.
実施例３ ウェスタン ブロッティング法による本発明の化合物の
性質の検討 １）モノクローナル抗体を用いた場合 従来、前述のＰＡＳ−ＯおよびＥＭＡの両方と反応する
ことが知られてるモノクローナル抗体３種［Ｍ８（Virc
hows Arch．Path．Anat．，294，279〜293，1982），Ｔ
Ｗ19.5（ヒトのモノクローナル抗体でLudwig Inst．for
Cancer ResearchのGore博士より提供を受けた）および
77.1（膀胱癌に対するモノクローナル抗体でThe Inst．
of Cancer Research（London）のSummerhays博士より提
供を受けた）］および115D8（Int．Ｊ．Cancer，34，19
7〜206，1984）を用いて本発明の糖蛋白質との反応性に
ついて検討した。Example 3 Examination of Properties of Compound of the Present Invention by Western Blotting Method 1) When Monoclonal Antibody is Used Conventionally, three kinds of monoclonal antibodies known to react with both PAS-O and EMA described above [M8 (Virc
hows Arch. Path. Anat. , 294 , 279-293, 1982), T
W19.5 (Ludwig Inst. For human monoclonal antibody
Provided by Dr. Gore of Cancer Research) and
77.1 (The monoclonal antibody to bladder cancer
donated by Dr. Summerhays of Cancer Research (London)] and 115D8 (Int. J. Cancer, 34 , 19).
7-206, 1984) was used to examine the reactivity with the glycoprotein of the present invention.
実験は実施例１に示した方法で電気泳動された本発明の
化合物およびＰＡＳ−Ｏをウェスタンブロッティング法
によりニトロセルロース膜（Bio−Rad社製）に転写装置
（ModelＡＥ−3280，アトー社製）で転写する。転写を
終了したニトロセルロース膜は0.9％塩化ナトリウム，
１％牛血清アルブミンと５％豚血清を含む１０ｍＭリン
酸バッファー，pH7.4でブロッキングし、次に各モノク
ローナル抗体を産出するハイブリドーマの培養上清と反
応させる。反応は最初４０℃，９０分間反応後４℃に冷
却し、一昼夜放置する。反応終了後１％牛血清アルブミ
ンおよび0.9％塩化ナトリウムを含む１０ｍＭリン酸バ
ッファー，pH7.4（１％ＢＳＡ／ＰＢＳ）でニトロセル
ロース膜を洗浄する。次に第２抗体として１％ＢＳＡ／
ＰＢＳで５００倍に希釈されたパーオキシターゼ結合抗
マウスＩｇＧ（ヤギ）を加え、４０℃，９０分反応させ
た。反応後再び１％ＢＳＡ／ＰＢＳで洗浄し、0.02％の
３，３′−ジアミノベンジジンおよび0.005％過酸化水
素を１０ｍＭリン酸バッファー，pH7.4で溶解した基質
中に移す。３０〜６０分間反応させニトロセルロース膜
上のバンドを検出する。その結果ＰＡＳ−ＯはＭ８，7
7.1，ＴＷ19.5および115D8のモノクローナル抗体に対し
て反応するが、本発明の糖蛋白質は全く反応しなかっ
た。In the experiment, the compound of the present invention electrophoresed by the method shown in Example 1 and PAS-O were transferred to a nitrocellulose membrane (manufactured by Bio-Rad) by a Western blotting method using a transfer device (Model AE-3280, manufactured by Atto). Transcribe. The transferred nitrocellulose membrane is 0.9% sodium chloride,
The cells are blocked with 10 mM phosphate buffer containing 1% bovine serum albumin and 5% swine serum, pH 7.4, and then reacted with the culture supernatant of the hybridoma producing each monoclonal antibody. The reaction is initially carried out at 40 ° C. for 90 minutes, cooled to 4 ° C., and allowed to stand overnight. After completion of the reaction, the nitrocellulose membrane is washed with 10 mM phosphate buffer containing 1% bovine serum albumin and 0.9% sodium chloride, pH 7.4 (1% BSA / PBS). Then, as the second antibody, 1% BSA /
Peroxidase-conjugated anti-mouse IgG (goat) diluted 500 times with PBS was added and reacted at 40 ° C. for 90 minutes. After the reaction, the plate is washed again with 1% BSA / PBS, and 0.02% 3,3'-diaminobenzidine and 0.005% hydrogen peroxide are transferred into a substrate dissolved in 10 mM phosphate buffer, pH 7.4. The reaction is carried out for 30 to 60 minutes and the band on the nitrocellulose membrane is detected. As a result, PAS-O is M8,7
It reacted with the monoclonal antibodies 7.1, TW19.5 and 115D8, but the glycoprotein of the present invention did not react at all.
２）レクチンを用いた場合 前述実施例３．１）に記載の方法と同様に処理し、転写
を終了したニトロセルロース膜はMoroi等の方法（Bioch
im．Biophys．Acta，798，295〜301、1984）に従いレク
チンとの反応性を検討した。用いたレクチンはパーオキ
シダーゼを結合したＰＮＡ，ＳＢＡ，ＷＧＡおよびConA
（いずれも生化学工業社製）を用いた。その結果本発明
の糖蛋白質は、ＰＮＡ，ＳＢＡおよびＷＧＡと反応し、
ConAとは反応しなかった。またＰＡＳ−ＯはＰＮＡおよ
びＷＧＡと反応したが他のレクチンとは反応しなかっ
た。2) In case of using lectin The nitrocellulose membrane treated by the same method as described in Example 3.1) above and the transfer of which has been completed is performed by Moroi et al.
im. Biophys. Acta, 798 , 295-301, 1984) and the reactivity with lectin was examined. The lectins used were peroxidase-bound PNA, SBA, WGA and ConA.
(All manufactured by Seikagaku Corporation) were used. As a result, the glycoprotein of the present invention reacts with PNA, SBA and WGA,
Did not react with ConA. PAS-O reacted with PNA and WGA but did not react with other lectins.
実施例４ 本発明の化合物の糖分析 本発明の化合物およびＰＡＳ−Ｏに含まれる中性糖は、
Clamp等の方法（Glycoproteins，300〜321，Elsevier P
ub．Co．，Amsterdam−London−New York）に従いトリ
メチルシリル誘導体とし、ガスクロマトグラフィーはシ
マズＧＣ−７Ａガスクロマトグラフ（シマズ社製）によ
り３％ＳＥ−３０／ChromosorbＷＨＰ（８０−１００メ
ッシュ）の条件で１３０℃から２００℃かつ２℃／min
のプログラムでおこなった。またヘキソーサミンは、あ
らかじめサンプルを４ＮＨＣｌで１００℃，６時間加水
分解し、日立８３５アミノ酸分析装置（日立社製）で分
析した。シアル酸は、シマズＬＣ−４Ａ高速液体クロマ
トグラフとZorbax ＮＨ2カラム（4.6×１５０mm）を使
い、５０％メタノールを含む２０ｍＭリン酸一アンモニ
ウム，pH2.66，３８℃の条件でクロマトグラフィーを行
い測定した。標準品としてはＮ−アセチルノイラミン酸
を用いた。その結果を次表に示す。表中Fuc，Gal，GlcN
Ac，GalNAcおよびＮＡＮＡとあるのはそれぞれフコー
ス，ガラクトース，Ｎ−アセチルグルコサミン，Ｎ−ア
セチルガラクトサミンおよびＮ−アセチルノイラミン酸
を示す。Example 4 Sugar Analysis of Compound of the Present Invention The neutral sugar contained in the compound of the present invention and PAS-O was
Methods such as Clamp (Glycoproteins, 300-321, Elsevier P
ub. Co. , Amsterdam-London-New York), and a trimethylsilyl derivative according to Gas Chromatograph (Shimazu GC-7A) (3-100% SE-30 / Chromosorb WHP (80-100 mesh)). And 2 ℃ / min
It was done with the program. For hexosamine, a sample was previously hydrolyzed with 4N HCl at 100 ° C. for 6 hours and analyzed with a Hitachi 835 amino acid analyzer (manufactured by Hitachi Ltd.). Sialic acid was measured by chromatography using a Shimadzu LC-4A high performance liquid chromatograph and a Zorbax NH 2 column (4.6 × 150 mm) under the conditions of 20 mM monoammonium phosphate containing 50% methanol, pH 2.66, and 38 ° C. did. N-acetylneuraminic acid was used as a standard product. The results are shown in the table below. Fuc, Gal, GlcN in the table
Ac, GalNAc and NANA represent fucose, galactose, N-acetylglucosamine, N-acetylgalactosamine and N-acetylneuraminic acid, respectively.
第１図には本発明の化合物のゲルろ過による流出パター
ンを示す。 第２図には本発明の化合物のアミノ酸分析の結果を示
す。FIG. 1 shows the outflow pattern of the compound of the present invention by gel filtration. FIG. 2 shows the result of amino acid analysis of the compound of the present invention.
Claims (3)
ァロース（Sepharose）ＣＬ−４Ｂカラムの排除限界を
越える高分子量を有し、アミノ酸分析では、セリンおよ
びスレオニンが他のアミノ酸と比較し1.4倍以上含ま
れ、糖含量の測定では糖を５０％以上含有する糖蛋白
質。1. A primate milk having a high molecular weight which exceeds the exclusion limit of a Sepharose CL-4B column, and in amino acid analysis, serine and threonine are compared with other amino acids in a molecular weight of 1.4. Glycoprotein that is more than doubled and contains 50% or more sugar in the measurement of sugar content.
第１項記載の糖蛋白質。2. The glycoprotein according to claim 1, which is obtained from human fat globule membrane.
項記載の糖蛋白質。3. Claim 1 obtained from human whey.
The glycoprotein according to the item.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP18367085A JPH0653760B2 (en) | 1985-08-21 | 1985-08-21 | High molecular weight glycoprotein in milk |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP18367085A JPH0653760B2 (en) | 1985-08-21 | 1985-08-21 | High molecular weight glycoprotein in milk |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS6243000A JPS6243000A (en) | 1987-02-24 |
| JPH0653760B2 true JPH0653760B2 (en) | 1994-07-20 |
Family
ID=16139871
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP18367085A Expired - Lifetime JPH0653760B2 (en) | 1985-08-21 | 1985-08-21 | High molecular weight glycoprotein in milk |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0653760B2 (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH11501996A (en) | 1995-03-14 | 1999-02-16 | キンバリー クラーク ワールドワイド インコーポレイテッド | Wettable articles |
-
1985
- 1985-08-21 JP JP18367085A patent/JPH0653760B2/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6243000A (en) | 1987-02-24 |
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