The Effect of Graded Doses of Secretin on Serum Trypsin,Serum Pancreatic Amylase,Serum Insulin,Plasma Somatostatin,and Plasma Pancreatic Polypeptide in Man

Six healthy men were studied with intravenous infusions of 0.3. 1.0, and 3.0 CU/kg-h of pure porcine secretin on separate days. The secretin elimination followed a first-order kinetics. Low pharmacological doses of secretin had no significant effects on blood levels of trypsin, pancreatic amylase, insulin, somatostatin, or pancreatic polypeptide (PP). whereas high pharmacological doses significantly elevated the blood levels of trypsin, pancreatic amylase, insulin, and somatostatin but were without effect on PP.     

Preparation and Properties of a Therapeutic Inter-Alpha-Trypsin Inhibitor Concentrate from Human Plasma

Inter-α-trypsin inhibitor (ITI) is a serine protease inhibitor found in human plasma. Its antiprotease activity is due to bikunin which is effective in various types of experimental shock and pancreatitis. Therefore ITI, which releases bikunin by proteolytic cleavage, could be of therapeutic interest. A method for the large-scale isolation of ITI from human plasma is described. ITI was purified from the prothrombin complex concentrate (PCC) by diethylaminoethyl-Sepharose fast-flow chromatography followed by a chromatographic step on immobilized heparin designed to remove C4, factor X and protein C. With this procedure, which was performed under mild conditions, a homogeneous preparation of native ITI was obtained, as demonstrated by electrophoretic and chromatographic analyses. ITI maintained its biological activity, as exhibited by its specific antitryptic activity of 420+65 IU/g. In order to decrease or eliminate the risk of transmission of viral disease due to lipid-enveloped viruses, the process incorporated a solvent-detergent treatment. Animal studies on the final product revealed no adverse side-effects in terms of toxicity, thrombogenicity or hypotension. This preparation appears suitable for therapeutic evaluation in animal experimental models.     

Inactivation of ''Arvin'' by Plasma Proteins

S ummary The coagulant activity of Arvin is neutralized by incubation with normal human serum. Coagulation experiments, and chromatographic and electrophoretic studies using radioactive Arvin, indicate that Arvin interacts with at least two serum proteins. One of these is α₂ macroglobulin and the other may be antithrombin III. Although these proteins inactivate thrombin also, the mechanisms of neutralization of Arvin and thrombin are not identical. In addition, considerable amounts of radio-active Arvin are trapped in the fibrin mesh when fibrinogen is clotted with Arvin. Serum samples from patients clinically resistant to Arvin showed complexing of Arvin with a γ globulin fraction, confirming the antibody nature of Arvin resistance.     

Serum Proteins Found in Primates

The serum proteins of seven primates are studied by immunoelectrophoresis using heterologons immune serums anti-Man, anti- Cynomolgus and anti-Lemur . The individual patterns are described and the homologies of a certain number of proteins were established with thofie of the reference species (Man, Cynomolgus and Lemur ). The electrophoretic mobilities of different proteins are calculated. Zoological implications are discussed.

Résumé

Les protéines sériques de sept espèces de primates ant été étudié es en immunoélectrophorèse au moyen d'immunsérums hétérologues anti-Homme, anti-Cyno molgus et anti- Lemur . Les images immnno-Clectrophoritiques sont décrites et les homologies de certaines protéines ant été établies avec celles des trois espèces de référence (Homme, Cynomolgus et Lémur ). Les mobilités électrophorétiques de différentes protéines ant été calculées. Les implications zoologiques sont discutées.

Zusammenfassung:

Mit Hilfe der Hetero-Immunseren Anti-Mensch, Anti-Cynomolgus iind Anti-Lemur wurden die Serumeiweiße von sieben Primaten immunoelektrophoretisch untersucht. Die einzeinen Immunoelektrophoresebilder wurden beschrieben; außerdem wurde die Homologie einer Reihe van Eiweißen niit denjenigen der Bezugsarten (Mensch, Cynomolgus und Lemur ) ermittelt. Die elektrophoretischen Beweglichkeiten verschiedener Eiweiße wurden berechnet. Die zoologischen Implikationen der Befunde werden diskutiert.     

Occlusion of Plasma Proteins by Human Fibrin: Studies using Trace-Labelled Proteins

S ummary The occlusion of 13 different proteins by human fibrin has been investigated using radioactive techniques. Each of the proteins examined exhibited different tendencies to be retained by clots. For a satisfactory demonstration of this, studies of the effects of varying protein and fibrinogen concentration were required and are reported here.
With normal plasma, the contamination of the syneresed and washed fibrins with albumin and transferrin was negligible whereas significant quantities of β-lipoproteins, haptoglobin-haemoglobin complex, free haemoglobin and IgG-globulins were trapped. Substantial contaminations were noted with macroglobulins (IgA, IgM and α₂-macroglobulin), and above all with plasminogen, of which more than 50 per cent was adsorbed to the fibrin. Bence Jones proteins were also occluded by fibrin, Type K more so than Type L, whereas iodinated thrombin showed no affinity for fibrin.
Some effects of clotting conditions on occlusion are also reported, and it is shown that in dilute plasmas occlusion is reduced and in covalently bound fibrin it is enhanced.     

Influence of Plasma Proteins on Erythrocyte Morphology and Sedimentation

The influence of plasma proteins on erythrocytes was studied by interference microscopy, scanning electron microscopy (SEM), and by Westergren erythrocyte sedimentation rate (ESR). Albumin kept erythrocytes dispersed as discoid spheres. Fibrinogen seemed responsible for the rouleaux phenomenon, but needed the co-influence of an immunoglobulin to induce rouleaux type of aggregates and high ESR. IgG, IgA and IgM caused immunologic type of aggregates. Albumin acted synergistically with fibrinogen and immunoglobulins. Normal blood contained a network of rouleaux, which probably explained the low normal ESR. High ESR was either due to rouleaux type aggregates where fibrinogen was dominant, or immunologic type aggregates where IgG, IgA or IgM were dominant proteins. Cold agglutinin disease showed normal blood morphology and normal ESR at 37°C and immunologic type aggregates and high ESR at 25°C.