Search results for: anti_Rat Haptoglobin
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Rat renal and plasma prorenin are activated in vitro by different mechanisms.
The aim of the present study was to purify and identify a plasma protein fraction (PreR-Co) involved in renal prorenin activation and to explore its capacity to process plasma prorenin. PreR-Co was obtained from plasma as a single electrophoretic band by (NH(4))(2)SO(4) precipitation, Sephacryl S-200 HR gel filtration, anti-rat albumin immunoaffinity, and ion-exchange chromatography. The amidase, esterase, and kallikrein activities of PreR-Co were studied, as was its N-terminal amino acid sequence. Rat kidney extract or plasma (normal or previously treated with acid to pH 2.8) were incubated with PreR-Co for 15 minutes at 37 degrees C. Renin concentration was measured by incubation with homologous angiotensinogen. The same protocol was repeated with samples activated by trypsin. The N-terminal amino acid sequence was IIGGSMDAKGSFP, which had a homology of 90% with the beta-chain of haptoglobin, 69% with serine-proteases, and 65% with kallikreins. The renin concentration in rat kidney extract was 34+/-4 ng of angiotensin I (Ang I). mg of tissue(-1). h(-1). After PreR-Co or trypsin treatments, renin concentrations were 211+/-7 and 110+/-11 ng of Ang I. mg of tissue(-1). h(-1), respectively. The plasma renin concentration in normal plasma was 67.6+/-13.3 ng of Ang I. mL(-1). h(-1), and no significant difference was observed after PreR-Co treatment. However, a significant increase (202.8+/-7.8 ng of Ang I. mL(-1). h(-1); P<0.01) was found after trypsin treatment. The isolated PreR-Co acts on renal prorenin but not on plasma prorenin. These results suggest that active renin is processed in the kidney by a circulating enzyme that may have a role in the regulation of circulating renin.P A Vincent, E De Vito
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Acute phase plasma proteins in kininogen-deficient Brown Norway rats.
We examined whether Brown Norway rat plasma (BN/May Pfd f) contains alpha 1-cysteine proteinase inhibitor (alpha 1-CPI), also called major acute phase alpha 1-protein or T-kininogen. T-kininogen is a low molecular weight kininogen from which kinin can be released by trypsin but not by kallikreins. The BN plasma reacted with rabbit anti-alpha 1-CPI gamma globulins. Purified alpha 1-CPI released a kinin-like activity with trypsin and with homogenate of salivary glands, as Brown Norway rat plasma did. High concentration of added rat urine induced a small release (10%) of kinin from alpha 1-CPI. Preincubation of Brown Norway rat plasma with rabbit anti-rat alpha 1-CPI gamma-globulins nearly suppressed the kinin-forming substrate of trypsin in this plasma. These results indicated that plasma of our Brown Norway rats contains only alpha 1-CPI as kinin-forming substrate. This plasma contains low amount of alpha 2-macroglobulin, while its content in orosomucoid and haptoglobin was a little larger than that of Wistar rat plasma.J Damas, R Vranckx, A Adam