Search results for: Haptoglobin Pig purified protein contfrol for Western
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Local identification of porcine haptoglobin in salivary gland and diaphragmatic muscle tissues.
In order to clarify the origin of the haptoglobin (Hp) quantified in saliva and meat juice samples, the extrahepatic localization of Hp in salivary gland and in diaphragmatic muscle, as part of the systemic acute phase response in pigs, was studied by immunohistochemistry. For this purpose a specific monoclonal antibody (mAb) produced by immunising mice with purified porcine Hp was used. Reactivity of the mAb was assessed by direct ELISA and by western blot, which showed the ability and specificity of the mAb to identify porcine haptoglobin as a purified antigen or in porcine serum in a native or denatured but non-reduced state. Five healthy and five diseased pigs were sampled at slaughter for serum and tissue procurement. Hepatic immunohistochemical analysis was used as control of the acute phase reaction status. In the liver, cell immunostaining revealed a perinuclear, cytoplasmic localization of Hp within hepatocytes, following mainly a periacinar pattern. Extrahepatic immunohistochemical analysis revealed positive cells in the glandular acini and duct epithelial cells of the salivary gland and intrasarcoplasmic immunolabelling of random diaphragmatic myofibers. A possible role of both salivary gland and diaphragmatic muscle on local Hp production could be postulated based on the present immunohistochemical study, which supports the concept that other cells besides hepatocytes may have the potential to produce Hp in the pig.A M Gutiérrez, J Yelamos, F J Pallarés, J Gómez-Laguna, J J Cerón
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Simple high-performance liquid chromatographic purification procedure for porcine plasma haptoglobin.
Haptoglobin is an acute-phase protein and its plasma levels increase consistently in response to infection and inflammation. Some evidence has demonstrated that haptoglobin is involved in the immune responses. In this study, we established a novel high-performance liquid chromatographic purification procedure for porcine plasma haptoglobin. The procedure required an ammonium sulfate fractionation and a HPLC Superose 12 gel-permeation chromatography. Purified porcine haptoglobin possessed one heavy (beta) and light chain (alpha) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, under reducing conditions, with a M(r) (molecular mass) of about 42,000 and 14,000 for heavy (beta) and light chains (alpha), respectively. Although the N-terminal amino acid sequence of porcine heavy chain of haptoglobin has never been reported previously, the analyses of N-terminal amino acid sequence showed a great sequence similarity to that of human and other animal species. In addition, Western blot using our specific antibody prepared against porcine M(r) 42,000 chain did react with human haptoglobin and likewise, the antibody against human haptoglobin also cross-reacted with purified porcine M(r) 42,000 chain. Thus, it confirmed that the identity of the porcine protein purified from our procedures was as haptoglobin.S J Yang, S J Mao