Search results for: Haptoglobin, Horse, purified protein
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Serum protein changes in grass sickness.
Polyacrylamide gel electrophoresis was used to compare serum taken from ponies before and during clinical illness confirmed as grass sickness. A consistent rise in the level of haptoglobin was seen in serum from animals which had shown symptoms for more than two days. Serum albumin was also shown to have altered mobility at the onset of clinical disease. Estimation of the haemoglobin-binding capacity confirmed the haptoglobin increase. This haptoglobin has been purified and some of its properties determined. In contrast to the situation in acute inflammatory conditions no other acute-phase proteins increased to a significant extent in grass sickness. It is concluded that the neurotoxin known to be present in sera of animals experiencing acute grass sickness cannot itself be detected by polyacrylamide gel electrophoresis but may be bound to serum albumin.P Johnson, A M Dawson, D L Mould
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96T1 Set1 Set1 Set1 Set5001mg96tests1 Set1 Set1 Set1 Set
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Microheterogeneity of mammalian haptoglobins in isoelectric focusing.
1. Human haptoglobin type 1-1, porcine haptoglobin, and equine haptoglobin were isolated and purified. 2. These haptoglobins were similar in polyacrylamide gel electrophoresis and in subunit structure but showed microheterogeneity in isoelectric focusing. 3. Isoelectric points of human haptoglobin as determined with photopolymerized gels were found to be 4.03-4.24, of porcine haptoglobin 4.0-4.30, and of horse haptoglobin 3.80-4.15, respectively. 4. Results obtained with chemically polymerized gels were 0.08-0.3 pH units higher. 5. Examined haptoglobins differed also in the ability of complex formation with hemoglobin, in sialic acid content and in antigenic specificity.W Dobryszycka, E Krawczyk
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100 UG1 Set10 mL100 μg1 Set4 Membranes/Box100 μg1 Set25
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Degradation and inactivation of ceruloplasmin and haptoglobin by rat liver lysosomes and some other proteinases.
Lysosomal fraction was isolated from rat liver by density gradient centrifugation after pervious loading of lysosomes in vivo with Triton WR-1339. Tritosome preparations were incubated at 37 degrees C and pH 5 for 24 hr with purified human ceruloplasmin or haptoglobin. After this period approximately 20% of total alpha amino nitrogen was released from ceruloplasmin and over 40% from haptoglobin. This was accompanied by loss of peroxidase activity of haptoglobin (in complex with haemoglobin), while enzymatic activity of ceruloplasmin remained unaltered. Removal of sialic acid by neuraminidase had no effect on digestion of ceruloplasmin by rat liver tritosomes. Both glycoproteins were resistant to horse leucocyte proteinases and pancreatic eleastase but were easily inactivated by trypsin and chymotrypsin.B Rostworowska