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Surfactant protein D (SP-D) is a collectin believed to play an important role in innate immunity. SP-D is characterized by having a collagen-like domain and a carbohydrate recognition domain (CRD), which has a specific Ca2+-dependent specificity for saccharides and thus the ability to bind complex glycoconjugates on micro-organisms. This paper describes the tissue immunolocalization of porcine SP-D (pSP-D) in normal slaughter pigs using a monoclonal antibody raised against purified pSP-D. Porcine SP-D was purified from porcine bronchoalveolar lavage (BAL) by maltose-agarose and immunoglobulin M affinity chromatography. The purified protein appeared on sodium dodecyl sulphate–polyacrylamide gel electrophoresis as a band of∼53 000 MW in the reduced state and∼138 000 MW in the unreduced state. Porcine SP-D was sensitive to collagenase digestion and N-deglycosylation, which reduced the molecular mass to∼24 000 MW and∼48 000 MW respectively, in the reduced state. N-deglycosylation of the collagen-resistant fragment, reduced the molecular mass to∼21 000 MW showing the presence of an N-glycosylation site located in the CRD. Porcine SP-D bound to solid-phase mannan in a dose and Ca2+-dependent manner with a saccharide specificity similar to rat and human SP-D. The purified protein was used for the production of a monoclonal anti-pSP-D antibody. The antibody reacted specifically with pSP-D in the reduced and unreduced state when analysed by Western blotting. Immunohistochemical evaluation of normal porcine tissues showed pSP-D immunoreactivity predominantly in Clara cells and serous cells of the bronchial submucosal glands, and to a lesser extent in alveolar type II cells, epithelial cells of the intestinal glands (crypts of Lieberkühn) in the duodenum, jejunum and ileum and serous cells of the dorsolateral lacrimal gland. [ABSTRACT FROM AUTHOR]

Twelve-day-old rats were fed a mixture of fast and slow chromato-graphically prepared fractions of bovine IgG, labelled with 125I and 131I. The pooled young rat sera were submitted to analysis by electrofocusing. The results show a wide variation of concentration quotients between the different pI peaks of IgG, with the more basic fractions being transmitted more readily in both fractions. One slow IgG peak (pI 7.8) in particular is transmitted very readily. These findings reinforce the concept of selectivity in transmission. The possible use of the young rat gut as a test for protein integrity is discussed. [ABSTRACT FROM AUTHOR]

The serum proteins of the grey squirrel have been examined quantitatively by fluid agar electrophoresis and free boundary electrophoresis, and qualitatively by the combined techniques of Porath zone electrophoresis, starch gel electrophoresis, immunoelectrophoresis, and Sephadex chromatography. At least seventeen proteins, differing antigenically, can be distinguished. Unlike other mammalian sera, squirrel serum is relatively rich in pre-albumin components, of which there are two. The fastest of these is a lipoprotein. Of the many proteins classed as α-2 globulins, two are macroglobulins. [ABSTRACT FROM AUTHOR]

Antiserum to a fraction of mouse β globulin isolated by electrophoresis and column chromatography was found receive by immunoflouresence with renal basement membrane of glomeruli and tubules, and with basement membrane and connective tissue in other organs. This method for staining renal basement membrane was applied to the study of renal lesions produced in mice by streptolysin S. In lesions characterized by early changes of acute tubular necrosis a marked decrease in ability to stain tubular basement membrane was observed. Reapperance of staining property in basement membrane was linked to regeneration of diseased tubules. Repeated injections of streptolysin S produced alterations in staining also of glomerular basement membrane [ABSTRACT FROM AUTHOR]

The electrophoretic patterns of six sera from rabbits immunized by two or more courses of intravenous injections of killed pneumococci type III showed multiple peaks in the γ-globulin region. Such sera contained large amounts of anti-body (up to 85 per cent of the total γ globulin) against the capsular polysaccharide. One serum contained a cryoglobulin, which contained almost as great a proportion of specific antibody as did the remaining γ globulin. The electrophoretic patterns and antibody contents were similar in the water-soluble and water-insoluble fractions of γ globulin. The sedimentation constant and diffusion coefficient of a water-soluble fraction of γ globulin, containing 85 per cent specific antibody, were measured. The values, at 0.4 per cent protein concentration, were S20.w=6.97 × 10-13 and D20.w= 4.16x10-7 cm.² sec.-1, corresponding to molecular weight 159,000. The antibody-containing globulin from one serum was separated by zone electrophoresis into three fractions with different electrophoretic mobilities. These contained 53–71 per cent of antibody precipitable by type III pneumococcus capsular polysaccharide. Only doubtfully, significant differences were found in respect of amino-acid composition, hexose and hexosamine contents, or antigenic characteristics. A method was devised for detecting small amounts of antibody against capsular polysaccharide by means of red cells sensitized with culture filtrates of capsulated pneumococci. The antibody was also fractionated by chromatography on anion-exchange cellulose, and numerous fractions with antibody activity were obtained. It was shown by labelling the γ globulin with 131xI that similar fractionation occurred both in the presence and absence of other serum components. All the chromatographic fractions of γ globulin were found to contain approximately similar proportions of antibody. By electrophoresis in starch gel the fractions were found to differ from one another and to be heterogeneous. The implications are discussed of the finding that antibody against type III pncumococcus capsular polysaccharide can occur over the entire range of γ-globulin molecules. [ABSTRACT FROM AUTHOR]

Human allergic serum has been fractionated by: Chromatography on diethyl amino ethyl cellulose columns. Ultracentrifugation in buffered sucrose gradients. Passive transfer tests with the fractions showed skin sensitizing activity to horse dandruff allergen to be associated with an electrophoretic gammax­globulin component possessing a 7S sedimentation constant. The difficulties encountered in the use of the chromatographic procedure for obtaining potent reagin preparations are discussed. [ABSTRACT FROM AUTHOR]