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Immunocytochemical Labeling of Enzymes in Low Temperature

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Immunocytochemical Labeling of Enzymes in Low Temperature Scanning Electron Microscopy Volume 4 Number 1 The Science of Biological Specimen Article 24 Preparation for Microscopy and Microanalysis 1985 Immunocytochemical Labeling of Enzymes in Low Temperature Embedded Plant Tissue: The Precursor of Glyoxysomal Malate Dehydrogenase is Located in the Cytosol of Watermelon Cotyledon Cells C. Sautter TU München, Weihenstephan Follow this and additional works at: https://digitalcommons.usu.edu/electron Part of the Biology Commons Recommended Citation Sautter, C. (1985) "Immunocytochemical Labeling of Enzymes in Low Temperature Embedded Plant Tissue: The Precursor of Glyoxysomal Malate Dehydrogenase is Located in the Cytosol of Watermelon Cotyledon Cells," Scanning Electron Microscopy: Vol. 4 : No. 1 , Article 24. Available at: https://digitalcommons.usu.edu/electron/vol4/iss1/24 This Article is brought to you for free and open access by the Western Dairy Center at DigitalCommons@USU. It has been accepted for inclusion in Scanning Electron Microscopy by an authorized administrator of DigitalCommons@USU. For more information, please contact [email protected]. Science of Biological Specimen Preparation (pp. 215-227) SEM Inc., AMF O'Hare (Chicago), IL 60666-0507, U.S.A. IMMUNOCYTOCHEMICALLABELING OF ENZYMES IN LOW TEMPERATUREEMBEDDED PLANT TISSUE: THE PRECURSOR OF GLYOXYSOMALMALATE DEHYDROGENASE IS LOCATEDIN THE CYTOSOLOF WATERMELONCOTYLEDON CELLS [.Sautter Lehrstuhl fur Botanik Fakultat fur Landwirtschaft und Gartenbau TU Munchen, Weihenstephan 8050 Freising, FRG Phone no.: 08161/71868 Abstract Introduction The Lowicryl-technique in combination with Immunocytochemical localization of enzymes is protein A gold was used in order to localize the well established in animal tissues. In plant precursor of glyoxysomal malate dehydrogenase in tissues immunocytochemistry was mainly restricted watermelon cotyledons. Preservation of the antigen to storage proteins (BAUMGARTNERet al. 1980; was evaluated by a preembedding technique in CRAIG and MILLERD1981; CRAIG and GOODCHILD1982; isolated organelles. The glyoxysomal malate CRAIG and GOODCHILD1984 a, 1984 b; GREENWOODet dehydrogenase was localized in tissue sections by al. 1984). Comparable few studies dealt with the a postembedding technique. Antigens of glyoxysomal localization of enzymes (DOMANand TRELEASE1985; malate dehydrogenase were found in the glyoxysomal SAUTTER 1984) regulatory proteins (VERBELENet al. matrix and in the cytosol, whereas the endoplasmic 1982), phytohormones (ZAVALAand BRANDON1983) or reticulum was completely free of labeling. inhibitors (HORISBERGERand TACCHINI-VONLANTHEN Controls are presented by preimmunserum, by a 1983 a, 1983 b). serum against various proteins of the glyoxysomal membr2ne and by application of cycloheximide in Plant tissues exibit special difficulties for order to inhibit translation at cytosolic immunocytochemistry. Most of these difficulties ribosomes. The results are compared with are due to the general differences between animal immunocytochemical localizations of other plant cells and plant cells. Cell walls usually do not microbody enzymes and of plant storage proteins. occur in animal tissues. They are a high diffusion barrier for macromolecules (KNOX1982), although for immunocytochemical localization of micro­ tubules preembedding techniques have been success­ fully used after cell wall digestion (WICK et al. 1981). Plants contain a variety of substances, which nonspecifically bind to immunoglobulins. Most important among these substances are lectins and certain glycoconjugates (KNOX 1982). These substances might cause considerable nonspecific labeling and thus severe problems in immuno­ cytochemistry. This difficulty can be completely avoided by preincubations with preimmunserum followed by incubation of protein A not coupled to gold particles (SAUTTER1984). Additionally problems are caused by fat storing tissue and heat labile enzymes. Immuno­ cytochemistry of cryosections of fat storing tissue is difficult, because during warming up of Key words: Immunocytochemistry, plant enzymes, the section, the unfixed lipid begins to flow over transmission electron microscopy, low temperature the section surface. This lipid covers antigenic embedding, glyoxysomes, malate dehydrogenase. determinants as well as the ultrastructure. Heat labile enzymes on the other hand prevent embedding in conventional epoxy resins, which need high temperatures for polymerization. The present study demonstrates localization of a plant enzyme in watermelon cotyledons. In this study the mentioned problems are combined: cell walls are present and do not allow for antibody diffusion (SAUTTER and HOCK 1982); 215 C. Sautter storage proteins are accumulated in protein bodies membrane was a gift from Dr. M. Conder (Univer­ and exhibit significant nonspecific binding sites sity of Warwick, England). for antibodies; watermelon cotyledons contain a high amount of storage lipid within their cells; Crude Homogenate glyoxysomal malate dehydrogenase (gMDH) the Although 1% glutaraldehyde for l hour led to enzyme to be localized - is heat labile (WALKand good immunolocalization of microbody marker HOCK1977b); furthermore, the interesting question enzymes (SAUTTER1984), this fixation protocol was was the localization of the precursor of this not useful for the preservation of gMDH-antigens. enzyme, which occurs only in low amounts within Therefore a preembedding technique was used in the cell. order to evaluate a fixation protocol, which preserves enough gMDH-antigens for immunocyto­ Conventional histochemistry is not useful in chemical detection. 120 cotyledons from 3 day old localizing gMDH and pre-gMDH because isoenzymes dark grown watermelon seedlings were homogenized exist and because enzyme precursors may be as described earlier (HOCK 1973). The enzymatically inactive. Thus immunocytochemistry homogenization medium contained 0.25M sucrose, is the technique of choice. Monospecific 50mM HEPES, 0.1?! (w/v) BSA, lOmM KCl, lmM antibodies against gMDH are available. They are MgCl2 , lmM Na2 -EDTA, lOmMDTE at pH 7.5 also able to recognize the pre-gMDH (GIETL and (WALKand HOCK1977 b). HOCK 1982). In order to avoid excessive heat damage of the heat labile gMDH(WALK and HOCK1977 For immunolabeling 80µ1 of a crude organelle b) Lowicryl was used as the embedding medium for fraction (10,000g pellet) was fixed for 15min at electron microscopy which is a successful room temperature. The fixative was added to the technique in immunolabeling of animal tissues organelle suspension. The fixed organelles were (ROTH et al. 1981). This technique has been used washed in homogenization buffer for 30min, with successfully for localization of microbody marker several changes; then 20µ1 anti-gMDH-serum was enzymes in watermelon cotyledons (SAUTTER1984). added. For controls, the anti-enzyme-serum was replaced by preimmunserum. The serum was allowed Materials and Methods to precipitate for l hour at room temperature and subsequently, for 4 hours at 50 C. Unbound Plant Material antibodies were washed out with homogenization Watermelon seeds (Citrullus vulgaris Schrad., buffer, which was changed several times at the var. Stone Mountain, harvest 1979) were obtained beginning. The last washing step was overnight at from Vaughan's Seed Company (Ovid, Michigan, USA). s0 c. A postfixation with 1% glutaraldehyde for After removing the seedcoat, the seedlings were l hour was followed by washing, dehydration and germinated at 30°C in the dark under sterile embedding as described for tissue. Antibodies were conditions on 0.8% agar as described by HOCK labeled at the surface of ultrathin sections with (1969). the following protocol: PBST ( see below) 5min; incubation of goat anti-rabbit ferritin coupled Preparation of Protein A Gold Complex (pAg) serum (Paesel, Frankfurt, FRG) diluted 1:20 with Colloidal gold particles (average diameter of PBST for 1 hour at room temperature; washing with 15nm) were prepared according to 8ENDAYANet al. PBST (15min, two changes) was followed by a wash (1980). An excess of protein A was applied for with water and counterstaining with uranyl acetate coupling. The uncoupled protein A was removed from for 7min. Lead counterstaining was omitted in this the conjugate by centrifugation. case. the same immunostaining was done with pAg diluted 1:20 instead of the secondary ferritin Sera coupled antibody. Monospecific anti-gMDH-serum was produced according to the methods of WALKand HOCK(1977 Under these conditions, fixation in 2.0% a). Monospecificity was tested by diffusion tests, formaldehyde and 0.2% glutaraldehyde preserved immunoelectrophoresis and by precipitation from enough gMDH-antigens for immunocytochemistry. The radiolabeled homogenates followed by SDS-gel result is shown on figs. 1-4 and on table 1. electrophoresis and fluorography. Polyspecific serum against various proteins of the glyoxysomal Table 1: Labeling of gMDH in isolated glyoxysomes. Sera anti-gMDH -serum preimmunserum difference _1) s.e.m. 2) -1) s.e.m. 6x 3 ) s .e .rn. s4l Markers xl 1 x2 2 Ferri tin 187.2 ± 16.8 36.5 ± 3.2 150.7 ± 17.1 0. 001 pAg 19.9 ± 3.9 1.6 ± 0.2 18.3 + 3.9 0.001 2 1) mean from at least 20 organelle profiles in markers per JJ-m section area 2) standard error of the mean 3) ti.~=xl-.x2 4) significance of Ax 216 Plant Enzymes .9 ,~·· .. f' I > g ~ - (?.Sµm 0.5µ \ ' A -,;. Figures 1-4: Crude organelle fraction. Fig.l: Preembedding labeling by anti-gMDH-serum, Fig.3: Preembedding labeling by anti-gMDH-serum, visualization by postembedding ferritin coupled
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