JP2006022038A - Method for producing soybean fermentation extract - Google Patents
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本発明は、大豆の発酵抽出物（fermented soybean extract、略称FSE）、特に、ナチュラルキラー細胞の活性及びγ―アミノ酪酸（ＧＡＢＡ）及びグルタミン酸の受容体との結合の阻害性を向上させるためのものを製造する方法に関する。 The present invention relates to fermented soybean extract (abbreviated as FSE), in particular, to improve the activity of natural killer cells and the inhibition of binding to receptors for γ-aminobutyric acid (GABA) and glutamic acid. It relates to a method of manufacturing.
単純アミノ酸ＧＡＢＡ及びグルタミン酸は、人の脳におけるそれぞれ抑制性、興奮性神経伝達物質である。脳において、全てではないとしても、大部分の神経細胞は、細胞外のＧＡＢＡ及びグルタミン酸に対する細胞膜受容体を有している。高い特異性を持つ輸送体（トランスポータ）は、これらのアミノ酸の細胞外の低い濃度を維持している。これらの輸送体はシナプスの周辺から放出されるＧＡＢＡ及びグルタミン酸を除く作用もあり、それらのシナプスでの作用を急速に停止させる。 The simple amino acids GABA and glutamate are inhibitory and excitatory neurotransmitters in the human brain, respectively. In the brain, most if not all neurons have cell membrane receptors for extracellular GABA and glutamate. Transporters with high specificity (transporters) maintain low extracellular concentrations of these amino acids. These transporters also have the effect of removing GABA and glutamate released from the periphery of the synapse, and rapidly stop their action at the synapse.
ＧＡＢＡは、三種類の異なるタイプの受容体、ＧＡＢＡA ，ＧＡＢＡB ，ＧＡＢＡc を活性化する。ＧＡＢＡA 受容体はリガンド依存性の塩素イオンチャンネルである。これらの受容体はＧＡＢＡ、ムシモル（muscimol）及びイソグバシン（isoguvacine ）により活性化され、ビスカカリン（biscuculline）、ガバジン（gabazine）及び（＋）−β−ヒドラスチン（hydrastine）により阻害される。
ＧＡＢＡA 受容体は大変重要であり、脳の興奮の調節において極めて重要な役割を担い、数多くの重要な薬剤、例えば、ベンゾジアゼピン（benzodiazepines ）、バービチュラテス（barbiturates) 、アルコール、ノイロステロイド（neurosteroids ）、いくつかの抗けいれん薬及び一般的麻酔剤などは、これら受容体と相互作用する。
GABA activates three different types of receptors, GABAA, GABAB and GABAc. The GABAA receptor is a ligand-dependent chloride channel. These receptors are activated by GABA, muscimol and isoguvacine and are inhibited by biscuculline, gabazine and (+)-β-hydrastine.
GABAA receptors are very important and play a pivotal role in the regulation of brain excitement, including many important drugs such as benzodiazepines, barbiturates, alcohol, neurosteroids, some Anticonvulsants and general anesthetics interact with these receptors.
グルタミン酸は二種の特異的な受容体と結合する。これらの受容体は関連するイオンチャンネル（イオンチャンネル共役型受容体）を開き、小さな陽イオンＮａ+ 及びＣａ+ を細胞内に向けて通過させる。いままで、三種のイオンチャンネル共役型受容体が確認されている。それらは、Ｎ−メチル−Ｄ−アスパルテート（N −methyl−D ―aspartate ）（ＮＭＤＡ），カイネート（kainate 、）及びα−アミノ−３−ヒドロキシ−５−メチル−４−イソオキサゾール・プロピオネート（α―amino -3- hydroxy -5- methyl -4- isoxazole propionate）（ＡＭＰＡ）である。グルタミン酸の変化は数多くのＣＮＳ病理症状と関連している。ＣＮＳ病理症状には、例えば、中風、大脳の漸次退化、慢性疼痛、憂鬱症、薬物依存症、てんかん、パーキンソン病及び精神分裂症などが含まれる。 Glutamate binds to two specific receptors. These receptors open the associated ion channel (ion channel coupled receptor) and allow small cations Na + and Ca + to pass into the cell. So far, three types of ion channel-coupled receptors have been identified. They include N-methyl-D-aspartate (NMDA), kainate, and α-amino-3-hydroxy-5-methyl-4-isoxazole propionate (α -Amino-3-hydroxy-5-methyl-4-isoxazole propionate) (AMPA). Changes in glutamate are associated with numerous CNS pathological symptoms. CNS pathological symptoms include, for example, moderate wind, progressive cerebral degeneration, chronic pain, depression, drug addiction, epilepsy, Parkinson's disease and schizophrenia.
本発明の主たる目的は、ナチュラルキラー細胞の活性を増進し、ＧＡＢＡ受容体及びグルタミン酸受容体との結合の阻害性を向上させるための大豆の発酵抽出物を製造する方法を提供することにある。
本発明の他の目的は、濃縮発酵液、すなわち有用な乳酸菌や酵母菌を用いて発酵した大豆発酵乳を提供することにある。
本発明のさらに別の目的は、直接に又はカプセル剤、錠剤もしくは水溶性粉剤として配合され、投与できる濃縮発酵液を提供することにある。
The main object of the present invention is to provide a method for producing a fermented soybean extract for enhancing the activity of natural killer cells and improving the inhibition of binding to GABA receptors and glutamate receptors.
Another object of the present invention is to provide concentrated fermented broth, that is, fermented soybean milk fermented using useful lactic acid bacteria and yeasts.
Yet another object of the present invention is to provide a concentrated fermentation broth that can be formulated and administered directly or as a capsule, tablet or water-soluble powder.
上記主目的を達成するため、本発明による大豆の発酵抽出物の製造方法は、次の工程からなることを特徴としている。
ａ．天然の栄養物を培養液に混ぜて、特殊な寒天培地を作る第１工程。
ｂ．第１工程で得られた寒天培地を制御環境に置いて個別に恒温で様々な種類の乳酸菌、酵母菌を培養する第２工程。
ｃ．第２工程で得られた乳酸菌、酵母菌及び前記寒天培地を該大豆培地に植菌し、制御条件下において恒温で全てのバクテリアを培養する第３工程。
ｄ．該乳酸菌、酵母菌を互いにグループごとに分離し、該有機大豆培地に移し、馴化、培養する第４工程。
ｅ．グループごとに培養した乳酸菌、酵母菌を該有機大豆培地に移し、共生的培養を開始し、大豆の発酵抽出物を得る第５工程。
In order to achieve the said main objective, the manufacturing method of the fermented soybean extract by this invention consists of the following processes.
a. The first step of creating a special agar medium by mixing natural nutrients with the culture solution.
b. A second step in which the agar medium obtained in the first step is placed in a controlled environment and various types of lactic acid bacteria and yeast are cultured individually at a constant temperature.
c. A third step of inoculating the lactic acid bacteria, yeasts and the agar medium obtained in the second step into the soybean medium and culturing all bacteria at a constant temperature under controlled conditions.
d. A fourth step in which the lactic acid bacteria and yeast are separated from each other in groups, transferred to the organic soybean medium, conditioned and cultured.
e. A fifth step of transferring lactic acid bacteria and yeast cultured for each group to the organic soybean medium, starting symbiotic culture, and obtaining a fermented soybean extract.
本発明の大豆の発酵抽出物の製造方法は、少なくとも、一種の乳酸菌、酵母菌を寒天培地に移送することを含む。抽出物の製造は、乳酸菌、酵母菌の共同培養、発酵から始まる。つまり、乳酸菌、酵母菌の馴化、培養を経たあと、濃縮液を作るステップが行われる。このプロセスに使われる微生物には、Lactobacillus paracasei 、Lactobacillus burglarious 、Saccharomyces cerivisiaeなどが含まれる。 The method for producing a fermented soybean extract of the present invention includes transferring at least one kind of lactic acid bacteria and yeast to an agar medium. The production of the extract starts with co-culture and fermentation of lactic acid bacteria and yeast. That is, a step of making a concentrated solution is performed after acclimatization and culture of lactic acid bacteria and yeast. Microorganisms used in this process include Lactobacillus paracasei, Lactobacillus burglarious, Saccharomyces cerivisiae and the like.
上記方法により製造される大豆の発酵抽出物は、これを人間に一定数量供給すると、ナチュラルキラー細胞の活性を増進させる外、γ―アミノ酪酸（GABA）受容体、アミノ酸（glutamate ）受容体を結合する能力があるので、抑制性を有する。大豆の発酵抽出物は、ＧＡＢＡ受容体及びアミノ酸（glutamate ）受容体に抑制性があるので、ペントバルビタール（pentobarbital ）から招いた睡眠時間を延長する。大豆の発酵抽出物は、化学療法期間中の癌患者の疲労感を軽減する。大豆の発酵抽出物は、カプセル状、錠剤状又は粉末状のいずれの形態でも形成することができる。 The fermented soybean extract produced by the above method enhances the natural killer cell activity when a certain amount is supplied to humans, and also binds γ-aminobutyric acid (GABA) receptor and amino acid (glutamate) receptor. Since it has the ability to Soybean fermented extract has an inhibitory effect on GABA and glutamate receptors, thus extending the sleep time incurred from pentobarbital. Soybean fermented extract reduces fatigue in cancer patients during chemotherapy. The soybean fermented extract can be formed in any form of capsule, tablet or powder.
本発明の目的、特徴及び効果などを良く理解するため、以下に、さらに具体的な実施例を図面を参照しながら説明する。
図１は、大豆の発酵抽出物のＩＣＲマウスの自発運動への影響を示すグラフ、図２は、大豆の発酵抽出物のペントバルビタールに誘起される睡眠時間への影響を示すグラフ、図３は、大豆の発酵抽出物のＧＡＢＡ受容体の結合への影響を示す表、図４は、大豆の発酵抽出物のアミノ酸（glutamate ）受容体の結合への影響を示す表、図５は、大豆の発酵抽出物の癌患者の化学療法期間中の食欲不振、疲労への影響を示す表である。
In order to better understand the objects, features and effects of the present invention, further specific embodiments will be described below with reference to the drawings.
FIG. 1 is a graph showing the effect of fermented soybean extract on locomotor activity of ICR mice, FIG. 2 is a graph showing the effect of fermented soybean extract on sleep time induced by pentobarbital, and FIG. FIG. 4 is a table showing the effect of soybean fermented extract on GABA receptor binding, FIG. 4 is a table showing the effect of soybean fermented extract on amino acid (glutamate) receptor binding, and FIG. It is a table | surface which shows the influence on anorexia and fatigue during the chemotherapy period of the cancer patient of a fermented extract.
図面に関して、若干の説明を加える。図３において、ＭＢＳがＧＡＢＡA に対して、ＩＣ50が０．０００７５％の稀釈濃度になると推量する。図４において、ＭＢＳ−２がＮＭＤＡ，ｋａｉｎａｔｅ受容体及び活性化剤に対して、ＩＣ50はそれぞれ０．０６９％、０．０９６％の稀釈濃度になると推量する。図５において、１０- ｃｍの視覚アナログ尺度（visual analog scale ）を採用する場合は、得点が高ければ、疲労の外、食欲も悪いことを表す。Ｐ値は、測定分析の反復を経て得られた。＊は、未服用のグループと比べると、０．０５の著しい差異があることを表す。＊＊は、未服用のグループと比べると、０．０１の著しい差異があることを表す。 Some explanation will be added to the drawings. In FIG. 3, it is presumed that the MBS is GABAA and the IC50 is a dilution of 0.00075%. In FIG. 4, it is presumed that MBS-2 has diluted concentrations of 0.069% and 0.096% for NMDA, kainate receptor and activator, respectively. In FIG. 5, when a 10-cm visual analog scale is employed, if the score is high, it means that the appetite is poor as well as fatigue. P values were obtained through repeated measurement analysis. * Represents a significant difference of 0.05 compared to the untreated group. ** represents a significant difference of 0.01 compared to the untreated group.
本発明の製造方法は、主に次の工程を含む。
（ア）培養液に天然の栄養源を混ぜ、特別な寒天培地を作る。
（イ）種々の乳酸菌、酵母菌を上記寒天培地に別々に接種し、それらを恒温、制御条件下に培養する。
（ウ）大豆を脱脂し、蒸留水を加え、約２時間煮沸し、大豆溶液を得、これをろ過し、有機培養液とする。
（エ）乳酸菌、酵母菌とステップ（イ）の培養菌液をそれぞれステップ（ウ）の大豆培養液に接種し、制御条件下、恒温で培養する。
（オ）グループずつで、乳酸菌、酵母菌をそれぞれステップ（ウ）の有機培養液に入れて訓化、培養させる。
（カ）ステッフ（オ）の各グループの培養液をステップ（ウ）で作られた大豆培養液に入れて、共生的に培養を開始する。
（キ）ステップ（カ）の微生物培養液を加熱し、高温で微生物の生長を終止させ、培養液の微生物を除く。また、ろ過液を元来の体積の十五分の一まで濃縮する（約９３％−９６％の水を除く）。
（ク）ステップ（カ）により作られた濃縮液を室温に少なくとも２ケ月置いて、濃縮液を分離させる。上層の液体を容器へ収集する。また、それを加熱して最終性生物を得る。 本生産工程において、異なる化学、製造、制御のグループの分析を行う。それはゲニスティン（genistein ）及びダイゼイン（daidzein）の含量、ＨＰＬＣの図案、ｐＨ値、物理性質（気味、外観、色、透明度、味覚、沈殿物）などを含む。
The production method of the present invention mainly includes the following steps.
(A) Mix a natural nutrient source with the culture solution to make a special agar medium.
(I) Various lactic acid bacteria and yeast are separately inoculated on the agar medium and cultured under constant temperature and controlled conditions.
(C) Degreasing soybeans, adding distilled water and boiling for about 2 hours to obtain a soybean solution, which is filtered to obtain an organic culture solution.
(D) Lactic acid bacteria, yeast, and the culture solution of step (i) are inoculated into the soybean culture solution of step (c), respectively, and cultured under controlled conditions at a constant temperature.
(E) In each group, lactic acid bacteria and yeast are put into the organic culture solution in step (c) and habituated and cultured.
(F) The culture solution of each group of step (e) is put into the soybean culture solution prepared in step (c), and the culture is started symbiotically.
(G) The microorganism culture solution in step (f) is heated to terminate the growth of microorganisms at a high temperature, and the microorganisms in the culture solution are removed. Also concentrate the filtrate to one-fifth of its original volume (excluding about 93% -96% water).
(H) The concentrate prepared in step (F) is allowed to stand at room temperature for at least 2 months to separate the concentrate. Collect the upper layer liquid in a container. It is also heated to obtain the final organism. In this production process, different chemistry, manufacturing and control groups are analyzed. It includes genistein and daidzein content, HPLC design, pH value, physical properties (flavor, appearance, color, transparency, taste, precipitate) and the like.
ＧＡＢＡ受容体とグルタミン酸受容体との結合力の試験管内分析：
本発明による濃縮発酵液のＧＡＢＡ受容体への作用は、放射線性リガンドを用いる結合活性試験により見積もる。本活性試験は、ＧＡＢＡA 受容体のアゴニスト部位への[3Ｈ]Muscimol の結合能を測量する。まずは雄Ｗｉｓｔａｒラットの小脳膜（重量１７５±２５ｇ）を、Tris-HCl、ｐＨ７．４緩衝液中に常法により準備する。それから、１０ｍｇの脳膜を１ｎＭ［3 Ｈ]Muscimol とともに４℃の温度で10分間培養する。１００ｎＭ[ 3 Ｈ]Muscimol の存在下で、非特異的な吸着量を算出する。脳膜を濾過し、３回洗浄し、フィルターの放射線量を計数することにより、特異的に結合した[3Ｈ]Muscimol を求める。
In vitro analysis of binding strength between GABA receptor and glutamate receptor:
The effect of the concentrated fermentation broth according to the present invention on the GABA receptor is estimated by a binding activity test using a radioligand. This activity test measures the ability of [3H] Muscimol to bind to the agonist site of the GABAA receptor. First, a cerebellar membrane (weight: 175 ± 25 g) of a male Wistar rat is prepared in a conventional manner in Tris-HCl, pH 7.4 buffer. Then 10 mg of brain membrane is incubated with 1 nM [ 3 H] Muscimol for 10 minutes at a temperature of 4 ° C. In the presence of 100 nM [ 3 H] Muscimol, non-specific adsorption amount is calculated. The brain membrane is filtered, washed three times, and the [3H] Muscimol specifically bound is determined by counting the radiation dose of the filter.
上述の放射線性標識体を用いる結合試験において、本発明の濃縮発酵液で実験を行った。本発明の抽出液ＩＣ50値は０．０００７５％の希釈濃度と算出された。このことにより、濃縮発酵液がＧＡＢＡのアゴニスト部位に対して強く結合することが示される。また、ＣＧＰ−３９６５３（選択的アンタゴニスト）のＮＭＤＡ受容体のアゴニスト部位への結合能力を測定することにより、本発明がアミノ酸（glutamate ）受容体に及ぼす影響を研究した。標準の実験ステップに基づいて、雄ラットの脳皮質の細胞膜を常法により分離した。２０ｍｇの調整した細胞膜と２．０。０ｎＭ［3 Ｈ］ＣＧＰ−３９６５３とともに、４℃の温度で２０分間培養した。そして、１０００μＭ Ｌ−glutamate 存在下での、非特異的な吸着量を求める。細胞膜を濾過し、緩衝液で３回洗った。フィルターの放射線量を計数することにより、 [3 Ｈ] ＣＧＰ−３９６５３の結合量を決定した。類似の実験により、リガンドとして５．０ｎＭ［3 Ｈ]kainateを使用し、グルタミン、kainate 受容体との結合能力を測定した。本発明の異なる稀釈濃度の抽出液で実験したところ、ＮＭＤＡ，ｋａｉｎａｔｅの二つ受容体に対して、本発明のＩＣ50は図４に示すように、それぞれ０．０６９％、０．０９６％となった。 In the binding test using the above-mentioned radioactive label, an experiment was conducted with the concentrated fermentation broth of the present invention. The IC50 value of the extract of the present invention was calculated as a dilution concentration of 0.00075%. This indicates that the concentrated fermentation broth strongly binds to the GABA agonist site. In addition, the influence of the present invention on the glutamate receptor was studied by measuring the ability of CGP-39653 (selective antagonist) to bind to the agonist site of the NMDA receptor. Based on standard experimental steps, the cell membranes of male rat brain cortex were separated by conventional methods. Cultured with 20 mg of conditioned cell membrane and 2.0.0 nM [ 3 H] CGP-39653 at a temperature of 4 ° C. for 20 minutes. Then, the amount of non-specific adsorption in the presence of 1000 μM L-glutamate is determined. The cell membrane was filtered and washed 3 times with buffer. The amount of [ 3 H] CGP-39553 binding was determined by counting the radiation dose of the filter. By a similar experiment, 5.0 nM [ 3 H] kainate was used as a ligand, and the binding ability with glutamine and kainate receptors was measured. As a result of experiments with different dilution concentrations of the present invention, the IC50 of the present invention was 0.069% and 0.096% for the two receptors, NMDA and kainate, as shown in FIG. It was.
ＩＣＲマウスにおいて、本発明の抽出液を投与すると、動物の活動力、ペントバルビタール（pentobarbital ）から誘起される睡眠時間への影響を調べた。
本発明の濃縮発酵液の経口投与（ヒト換算で１３ｍｌ量）によりマウスの自発運動を顕著に低下させ、また、ペントバルビタールにより誘起された睡眠時間も延長した（図１、図２参照）。
本発明の人体の臨床試験としては、１０−ｃｍの視覚的アナログ尺度（visual analog scale ）を採用すれば、本案の抽出液を服用すれば、１４〜２８日を経て、癌患者の疲労感を著しく軽減し、食欲も大いに増進される（図５参照）。
In ICR mice, when the extract of the present invention was administered, the effects on the activity of animals, sleep time induced by pentobarbital were examined.
Oral administration of the concentrated fermented liquid of the present invention (13 ml amount in terms of human) markedly decreased the spontaneous movement of mice and also prolonged the sleep time induced by pentobarbital (see FIGS. 1 and 2).
As a clinical trial of the human body of the present invention, if a 10-cm visual analog scale is adopted, if the extract of the present proposal is taken, it will take 14 to 28 days, and fatigue of cancer patients will be felt. It is significantly reduced and appetite is greatly enhanced (see FIG. 5).
Claims (6)
ａ．天然の栄養物を培養液に混ぜて、特殊な寒天培地を作る第１工程。
ｂ．第１工程で得られた寒天培地を制御環境に置いて個別に恒温で様々な種類の乳酸菌、酵母菌を培養する第２工程。
ｃ．第２工程で得られた乳酸菌、酵母菌及び前記寒天培地を該大豆培地に植菌し、制御条件下において恒温で全てのバクテリアを培養する第３工程。
ｄ．該乳酸菌、酵母菌を互いにグループごとに分離し、該有機大豆培地に移し、馴化、培養する第４工程。
ｅ．グループごとに培養した乳酸菌、酵母菌を該有機大豆培地に移し、共生的培養を開始し、大豆の発酵抽出物を得る第５工程。 The manufacturing method of the fermented extract of soybean including the following processes.
a. The first step of creating a special agar medium by mixing natural nutrients with the culture solution.
b. A second step in which the agar medium obtained in the first step is placed in a controlled environment and various types of lactic acid bacteria and yeast are cultured individually at a constant temperature.
c. A third step of inoculating the lactic acid bacteria, yeasts and the agar medium obtained in the second step into the soybean medium and culturing all bacteria at a constant temperature under controlled conditions.
d. A fourth step in which the lactic acid bacteria and yeast are separated from each other in groups, transferred to the organic soybean medium, conditioned and cultured.
e. A fifth step of transferring lactic acid bacteria and yeast cultured for each group to the organic soybean medium, starting symbiotic culture, and obtaining a fermented soybean extract.
The method for producing a fermented extract of soybean according to claim 1, wherein the fermented extract has a capsule, tablet, or powder form.
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007088905A1 (en) | 2006-01-31 | 2007-08-09 | Matsushita Electric Industrial Co., Ltd. | Blood test method and blood test apparatus |
| JP2008228654A (en) * | 2007-03-20 | 2008-10-02 | Kigen Biogenics Kenkyusho:Kk | Fermented food doubling as culture medium, and method for producing the same |
| JP2015051970A (en) * | 2013-09-06 | 2015-03-19 | マイクロバイオ カンパニー， リミテッド | Composition for producing adjuvant for cancer patients receiving chemotherapy |
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| JPH11103825A (en) * | 1997-08-08 | 1999-04-20 | Tochigi Pref Gov | Production of food rich in gamma-aminobutyric acid using aspergillus oryzae |
| WO2001093696A1 (en) * | 2000-06-02 | 2001-12-13 | Ikeda Food Research Co., Ltd. | PROCESS FOR PRODUCING FERMENTED FOODS RICH IN η-AMINOBUTYRIC ACID AND FREE AMINO ACIDS |
| JP2002255840A (en) * | 2001-02-27 | 2002-09-11 | Rheology Kino Shokuhin Kenkyusho:Kk | Cancinogenesis inhibitor |
| JP2003012534A (en) * | 2001-06-25 | 2003-01-15 | Busshin Kagaku:Kk | Enzyme activity inhibitor |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH11103825A (en) * | 1997-08-08 | 1999-04-20 | Tochigi Pref Gov | Production of food rich in gamma-aminobutyric acid using aspergillus oryzae |
| WO2001093696A1 (en) * | 2000-06-02 | 2001-12-13 | Ikeda Food Research Co., Ltd. | PROCESS FOR PRODUCING FERMENTED FOODS RICH IN η-AMINOBUTYRIC ACID AND FREE AMINO ACIDS |
| JP2002255840A (en) * | 2001-02-27 | 2002-09-11 | Rheology Kino Shokuhin Kenkyusho:Kk | Cancinogenesis inhibitor |
| JP2003012534A (en) * | 2001-06-25 | 2003-01-15 | Busshin Kagaku:Kk | Enzyme activity inhibitor |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007088905A1 (en) | 2006-01-31 | 2007-08-09 | Matsushita Electric Industrial Co., Ltd. | Blood test method and blood test apparatus |
| JP2008228654A (en) * | 2007-03-20 | 2008-10-02 | Kigen Biogenics Kenkyusho:Kk | Fermented food doubling as culture medium, and method for producing the same |
| JP2015051970A (en) * | 2013-09-06 | 2015-03-19 | マイクロバイオ カンパニー， リミテッド | Composition for producing adjuvant for cancer patients receiving chemotherapy |
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