SCIE
SCOPUS
KCI등재
Self - protective Activity of Colostral IgA Globulin from Tryptic Digestion
저자
Kim, Woo Jung (Department of Biochemistry, Catholic Medical College) ; Kang, Yoon Se (Department of Biochemistry, Catholic Medical College) ; Shim, Bong Sop (Department of Biochemistry, Catholic Medical College) ; Cho, Sung Hoon (Department of Biochemistry, Catholic Medical College) ; Lee, Du Bong (Department of Biochemistry, Catholic Medical College)
발행기관
생화학분자생물학회(Korean Society for Biochemistry and Molecular Biology)
학술지명
권호사항
발행연도
1971
작성언어
English
KDC
472
등재정보
SCIE,SCOPUS,KCI등재
자료형태
학술저널
발행기관 URL
수록면
6-8(3쪽)
제공처
Although the amount of IgA in serum is small compared with the amount of IgG, IgA is redominant in secretory fluids such as colostrum, saliva, nasal fluid and tears. IgA from the colostrum and saliva has a higher sedimentation constant (11S) than serum IgA(7S), and 11S colostral IgA has additional antigenic determinants with specificities which are not present in serum IgA. In addition to the heavy and light chains present in the molecule of serum IgA, colostral IgA has another protein component-the transport piece or the secretory piece.
Immune globulin in colostrum accounts for the immunity to certain infections acquired by newborn mammals after suckling. After hydrolysis in the gut, proteins in the form of aminoacids are thought to be absorbed, but there is -no experimental evidence for this. We have therefore studied the problems as follows. Colostrum was collected after delivery from primiparous women, and colostraI IgA was purified by gel filtration with Sephadex G-200 and DEAE-cellulose chromatography according to the method of Cebra and Robins. Antitryptic activity was measured in two ways. First, the inhibitory capacity of whole colostrum against trypsin was performed as described by Faarvang using urea-denatured bovine hemoglobin solution as substarate. Fifty microliters of a 0.2 per cent solution of crude trypsin was warmed at 25 for 20 minutes in a water bath. One hundred and fifty microliters of fresh whole colpstrum, prewarmed to 25 or 150 microliters of human serum was added to the above prewarmed enzyme solution. Two minutes later 0.5 ㎖ of 22 per cent urea-denatured bovine hemoglobin solution and 100 microliters of 0.1 M phosphate buffer, pH 8.0, were added, and the mixture was incubated for 20 minutxs at 25° The undigested protein was then precipitated by 2.5 ㎖ of 0. 3 M trichloroacetic acid. After the mixture had been centrifuged or filtered, 50 microliters of the supernatant was used for the Folin-Ciocalteu reaction. Trichloroacetic acid was added to the blank before addition of the hemoglobin solution, and the absorbance was read at 700 mmicrons with a Beckman DU-2 spectrophotometer.
The second method which we followed was as described by Kueppers and Bearn. One part pf 0. 1 per cent bovine fibrinogen in 0.1 M phosphate buffer, pH 8.0, ,was mixed with ten parts of 2 per cent hot agar (80-90°in 0.1 M phosphate buffer, pH 8. 0. On mixing the fibrinogen with hot agar the mixture immediately turned cloudy and it was poured onto a glass slide which was kept in a moist chamber for one hour. A longitudinal strip of agar, 3 mm wide, was then cut out to make a trough, and near the trough two wells, 0.4 mm ;in diameter, were punched out of the agar. The trough was filled with 0.2 per cent crLde trypsin solution in 0.1 M phosphate buffer, pH 8. 0. One hundred microliters of fresh human colostrum or isolated colostral IgA or fresh human serum were introduced side by side into the wells and the slide was left overnight at 40 in a moist chamber. After washing the slide with 0.15 M NaCl to remove the digested fibrinogen peptides, it was stained with amidoblack 10B.
Using hemoglobin as substrate, colostrum-unlike serum-did not show antitryptic activity. When, however, either colostrum or colostral IgA was tested using the fibrinogen-agar-gel slide technic, it showed antitryptic activity similar to that shown by serum.
The discrepancy between the two results can be explained as follows. Serum antitrypsin acts. directly on the trypsin molecule, thus protecting every kind of protein molecule from tryptic digestion. Colostral IgA on the other hand has only self-protecting activity against trypsin. Thus when hemoglobin was used as substrate there was no antitrypticactivity, whereas in the fibrinogen-agar-gel slide technic antitryptic activity was evident because colostral IgA which cannot be digested by trypsin diffused through the fibrinogen-agar medium. From the theoretical point of view also, colostral antibody should not interfere with the digestion of other nutritionally important proteins in the milk and. it should have only self-protective action for absorption or for its biologic activity in the gut.
The presence of antitrypsin in colostrum was thought to aid passive alimentary immunity by delaying they hydrolysis of antibody. Chamberlain and others, however, failed to show the absorption of gamma globulin intact in piglets after experimental addition of antitxypsin. It may be then that passive immunity is aided only by the antitryptic activity of specific, intrinsic colostral IgA.
At the present time we do not know whether the whole intact IgA molecule or only that part which retains the antibody activity is protected from tryptic digestion. Serum IgA and. colostral IgA differ in the presence of the so-called transport piece in the calostral IgA molecule. We have demonstrated the presence of the additional protein component in the colostral IgA. by gel filtration of reduced and alkylated colostral IgA, so it seems reasonable to assume that one possible function of the transport piece is to protect the molecule or the part of the molecule which has the antibody activity from proteolytic enzymes in the gut. Direct demonstration of the antitryptic activity of the transport piece is now under progress.
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