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한국 재래산양유 및 혈청중의 Immunoglobulin G 의 함량에 관한 연구 1 . 비유기간에 따른 IgG 의 함량변화
하월규,임종우,최충국 ( Woel Kyu Ha,Jong Woo Lim,Chung Kug Choi ) 한국축산학회 1986 한국축산학회지 Vol.28 No.10
To investigate the changes of IgG concentration in colostra, normal milk and blood serum, this experiment was carried out with Korean Native Goats for 21 days postpartum. Samples were collected at 0, 12, 24, 36, 48, 72, 96, 120, 144, 168 hrs and in 3 days interval from 10 to 21 days after parturition. The results obtained were as follows: 1. IgG concentration in colostrurn at the first milking postpartum were significantly (P$lt;0.05) decreased for 48 hrs postpartum in primipara and 24 hrs postpartum in multipara, respectively. 2. IgG concentration in blood serum from colostral period to normal lactation stages were significantly increased (P$lt;0.05) in primipara and multipara. 3. The IgG concentration in milk showed significantly (P$lt;0.01) negative correlationship with that of blood serum (r=-0.2697).
하월규 ( Woel-kyu Ha ),이정민 ( Jeongmin Lee ),김규언 ( Kyu-earn Kim ) 대한천식알레르기학회(구 대한알레르기학회) 2017 Allergy Asthma & Respiratory Disease Vol.5 No.2
Milk proteins are composed of casein, further classified into αS1-casein, αS2-casein, β-casein, and κ-casein, and whey protein, which is separated into α-lacatalbumin, β-lactoglobulin, serum albumin, and some minor proteins, such as lactoferrin and immunoglobulin. To reduce the allergenicity of protein, heat treatment and enzymatic protein hydrolysis by endopeptidase are necessarily required. Additionally, membrane technology should be applied to produce a protein hydrolyzate, which has consistent molecular weight of peptide and low in free amino acid without allergenic peptide or protein. Extensive casein hydrolyzate and whey protein hydrolyzate are used for protein source of mainly extensively hydrolyzed protein formula (eHF) intended for the treatment of cow`s milk allergy. Also, partially hydrolyzed formula (pHF) is developed, which is using a single protein source e.g., whey protein hydrolyzate. The allergenicity of infant formula can be determined according to molecular weight profile and antigenicity reduction compared to intact protein. More than 90% peptides are present in eHF have a molecular weight of < 3,000 Da. Peptide molecular weight profiles of pHF range mainly between 3,000 and 10,000 Da, but have a small percentage of >10,000 Da. Generally, antigenicity reduction in eHF and pHF is 10<sup>-6</sup> and 10<sup>-3</sup>, respectively. Even if protein hydrolyzate is manufactured under strict quality control, there is still a risk of cross contamination of allergenic milk components through environmental conditions and the shared manufacturing process. Thus, quality assessment of protein hydrolyzate formula must be performed routinely. (Allergy Asthma Respir Dis 2017:5:63-72)
토끼 항 ${\beta}-Lactoglobulin$ 항혈청에 대한 유청단백질 가수분해물의 항원성
이수원,하월규,전석락,김정완,손동화,이재영,Lee, Soo-Won,Ha, Woel-Kyu,Juhn, Suk-Lak,Kim, Jung-Wan,Shon, Dong-Hwa,Lee, Jae-Young 한국식품과학회 1994 한국식품과학회지 Vol.26 No.5
Chymotrypsin, trypsin, pancreatin, 그리고 Aspergillus oryzae 유래 단백질분해효소의 in vitro 처리에 의하여 유청단백질(WPI)의 가수분해물(WPH)중 ${\beta}-LG$유래의 항원성변화를 조사하기 위하여 토끼 항${\beta}-LG$항혈청을 이용한 competitive inhibition ELISA(cELISA)와 heterologous PCA를 실시하였다. cELISA에 의하여 WPH의 monovalent항원성을 분석한 결과, 전체적으로 ${\beta}-LG$유래의 monovalent항원성은 효소처리에 의하여 $10^{-1.7}{\sim}10^{-4.1}$배 또는 그 이하로 저하되었으며, 특히 pepsin전처리후 Asp. oryzae유래의 효소로 가수분해한 경우(OUP)의 항원성은 거의 상실되었다. Guinea pig를 이용한 PCA test에 의하여 ${\beta}-LG$유래의 polyvalent항원성을 분석한 결과, WPH의 항원성은 $1/2{\sim}1/128$ 또는 그 이하로 저하되었다. 특히, WPH중에서 열변성이나 pepsin의 전처리없이 Asp. oryzae유래의 효소로 가수분해한 경우(OUN), 가수분해도(DH)가 그다지 높지 않고 monovalent항원성도 여전히 잔존하였음에도 불구하고($10^{-3.2}$배로 저하) 알레르기의 발증과 밀접한 관련이 있는 polyvalent항원성은 거의 상실되었다. 이는 OUN의 분해효율이 아주 높지는 않으나 ${\beta}-LG$상의 항원결정기가 효과적으로 파괴되어, polyvalent항원성이 제거되었기 때문으로 추측된다. 이 결과는, Asp. oryzae유래의 효소를 WPI에 처리하면 우유 알레르기의 주요 원인물질인 ${\beta}-LG$의 polyvalent항원성이 제거됨으로써 저알레르기성 infant formula용 WPH가 제조될 수 있음을 시사하고 있다. In order to investigate the lowering effects of in vitro enzymatic hydrolysis by the treatment of chymotrypsin, trypsin, pancreatin, or protease from Aspergillus oryzae on the antigenicity of whey protein(WPI) against rabbit anti ${\beta}-LG$ antiserum, competitive inhibition ELISA(cELISA) and passive cutaneous anaphylaxis(PCA) test using guinea pig were performed. The results of cELISA showed that the monovalent antigenicity of the whey protein hydrolysates(WPH) to the antiserum was decreased to $10^{-1.7}{\sim}10^{-4.1}$ and less by the hydrolysis. Especially, the antigenicity of OUP(hydrolysate by protease from Asp. oryzae with preteatment of pepsin) was found almost to be removed. By the heterologous PCA the polyvalent antigenicity of the WPH was decreased to $1/2{\sim}1/128$ and less. Especially, the polyvalent antigenicity of OUN(hydrolysate by protease from Asp. oryzae without preteatments) was found almost to be removed, although OUN did not have so high degree of hydrolysis(DH) or so low monovalent antigenicity (reduced to $10^{-3.2}$). Therefore, this result was assumed to come from effective destruction of antigenic determinants on ${\beta}-LG$ in WPI, not to produce polyvalent antigenic peptides that are closely associated with induction of allergy. This finding suggested that WPH prepared by the treatment of microorganic protease from Asp. oryzae would be a material for hypoallergenic infant formula due to the removal of the polyvalent antigenicity of ${\beta}-LG$, the major milk allergen in WPI.
한우와 젖소 초유로부터 분리한 Lactoferrin의 생화학적 특성
양희진,손동화,하월규,이수원,Yang Hee-Jin,Son Dong-Hwa,Ha Woel-Kyu,Lee Soo-Won 한국축산식품학회 2005 한국축산식품학회지 Vol.25 No.1
본 연구는 우리나라 재래종인 한우로부터 초유를 얻어 Lf을 분리·정제한 후 한우 Lf의 생화학적 특성을 확인하였다. 정제된 한우 Lf은 분자량이 81,000Da이고 등전점은 pI 9였으며, 철함량이 0.56 mg/g으로 철 포화도는 약 40.6%로 측정되었다. 한우 Lf과 젖소 Lf은 아미노산 조성과 a-helix 함량에서 서로 다르게 나타났다. 또한, 항원 항체 반응으로 확인한 결과, K-Lf과 B-Lf 간에는 교차반응을 보였으나 H-Lf과는 교차반응을 보이지 않았다. The purpose of this study was to demonstrate biochemical properties of lactoferrin (Lf) obtained from the colostrum of Korea native cow. The molecular weight of the purified Korean native cow's Lf (K-Lf) was 81kDa, the isoelectric point was 9, and the content of iron was 0.56 mg/g, which is indicated that iron saturation of the lactoferrin was 40.6%. Amino acid composition and a-helix content were different K-Lf from bovine Lf (B-Lf). Immunological cross reactivity was observed between K-Lf and B-Lf but not between K-Lf and human Lf (H-Lf) by immunodiffusion test and Western blot analysis. Out results indicate that structure of K-Lf is different from that of B-Lf although K-Lf and B-Lf were immunologically cross-reactive.