Comparative Study of Proactivators of the Fibrinolysin System in Three Mammalian Species

1969 ◽  
Vol 21 (03) ◽  
pp. 594-603 ◽  
Author(s):  
Y Takada ◽  
A Takada ◽  
J. L Ambrus
Keyword(s):  
Guinea Pig ◽  
Comparative Study ◽  
Human Plasma ◽  
Mammalian Species ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
The Other ◽  
Rabbit Plasma ◽  
Plate Test ◽  
Fibrin Plate

SummarySephadex gel filtration of human plasma gave results suggesting the presence of two proactivators of plasminogen, termed proactivators A and B.Activity resembling that of proactivator A was found in rabbit plasma, but not in guinea pig plasma.Plasminogen activators produced by the interaction of proactivator A of human plasma with streptokinase had no caseinolytic or TAMe esterolytic effect.Proactivator A can be separated in a form apparently free from plasminogen, as shown by the heated fibrin plate test and by immunological analysis. On the other hand, proactivator B concentrates prepared so far are contamined with plasminogen.Human proactivators appear to be far more susceptible to streptokinase than are rabbit proactivators.Inhibitors of the fibrinolysin system were observed in the plasmas of all 3 species. These inhibitors are not present in the euglobulin fraction of plasma. Sephadex fractionation of euglobulin fractions results in proactivator preparations that do not contain inhibitors.

Distinction of Plasma Inhibitor of Activator-Induced Clot Lysis from Antiplasmins

1975 ◽  
Author(s):  
N. Aoki ◽  
M. Matsuda ◽  
M. Moroi ◽  
N. Yoshida
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
Inhibitory Effect ◽  
Clot Lysis ◽  
Plasminogen Activation ◽  
Lysis Time ◽  
Α2 Macroglobulin ◽  
Clot Lysis Time

A fraction of human plasma prolongs the activator-induced clot lysis time and inhibits plasminogen activation by the plasminogen activators derived from various sources (urine and tissues). This fraction, designated as antiactivator fraction, was separatid from antiplasmin fractions (α2-macroglobulin and α1-antitrypsin) by gel filtration and affinity chromatography on Sepharose coupled with IgG of antiserum to α1-antitrypsin. Anti-activator fraction thus obtained exerted little antiplasmin activity but inhibited strongly activator-induced clot lysis.Inhibitory effect of plasma on urokinase-induced clot lysis (antiactivator activity) was assayed in various diseases and compared with antiplasmin activity. No correlation was found between the two activities, and it was concluded that the two activities are independent and are ascribed to two different entities.

Effects of Epinephrine, Norepinephrine and Isopropylarterenol on the Isolated Auricles of Four Mammalian Species

1956 ◽  
Vol 185 (2) ◽  
pp. 332-336 ◽  
Author(s):  
Solomon Garb ◽  
Mario Penna ◽  
Aaron Ganz
Keyword(s):  
Cardiac Arrest ◽  
Adrenal Gland ◽  
Guinea Pig ◽  
Mammalian Species ◽  
The Other ◽  
Dilute Solutions ◽  
Species Response ◽  
Bioassay Technique ◽  
The Right ◽  
Great Potency

Epinephrine, norepinephrine and Isuprel were tested on the amplitude of contraction and rate of the auricles of the rat, guinea pig, rabbit and cat. In all species Isuprel was much more potent in its effects than the other amines. In the rat auricle Isuprel dilutions of 1 part in 20 trillion produced marked changes in rate and amplitude. Norepinephrine was the least potent of the three amines. The right auricle was more sensitive than the left. The great potency of Isuprel suggests that even the small concentrations of it or a similar amine which Lockett (1) reported finding in the adrenal gland would produce marked changes in auricular function. Therefore, it may be physiologically important. The ability of dilute solutions of Isuprel to restore a rapid spontaneous beat to an asystolic auricle suggests a possible role in the management of cardiac arrest. The marked differences in species response to the three amines may make this a useful bioassay technique. The combination of rat and guinea pig auricles should distinguish between the three amines in dilute solutions.

Characteristics of auto-antibodies to bovine TSH in the serum of two patients with Graves' disease

1983 ◽  
Vol 104 (4) ◽  
pp. 423-430 ◽  
Author(s):  
Yoshihiro Kajita ◽  
Yoshiyuki Nakajima ◽  
Masao Ishida ◽  
Yukio Ochi ◽  
Tadayoshi Miyazaki ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Mammalian Species ◽  
Gel Filtration ◽  
Binding Activity ◽  
The Other ◽  
Graves Disease ◽  
Antibody Method ◽  
Polyclonal Immunoglobulin ◽  
Auto Antibody ◽  
Bovine Tsh

Abstract. In this report we describe the characteristics of auto-antibodies to bovine TSH (bTSH) detected in the serum of 2 females among 102 patients with Graves' disease. These patients had never been injected with bTSH. One patient had high LATS activity and high bTSH binding activity after isotope therapy. The other patient showed no detectable LATS activity. Interestingly, the antibody showed a specifically high binding activity for the labelled TSH preparation purified by receptor. The auto-antibody could be demonstrated by the double antibody method, polyethylene glycol method, and by gel-filtration. The antibody was polyclonal immunoglobulin G (IgG). Because the binding of [125I]bTSH with the patient's antibody was inhibited by pituitary extracts from mammalian species other than human, this antibody may cross-react with bovine, rat, dog, rabbit and whale TSH. Although the incidence of the antibody in Graves' disease is low and the pathological significance remains obscure, the existence of this antibody in the serum of patients may suggest that autoimmune mechanisms may involve not only the thyroid but also the pituitary in Graves' disease.

DISTRIBUTION OF THE TWO TYPES OF A CELLS IN THE PANCREATIC ISLETS OF SOME MAMMALIAN SPECIES

1964 ◽  
Vol 46 (2) ◽  
pp. 307-316 ◽  
Author(s):  
Gunnar Alm ◽  
Bo Hellman
Keyword(s):  
Guinea Pig ◽  
Pancreatic Islets ◽  
Considerable Increase ◽  
Mammalian Species ◽  
Cell Number ◽  
The Other ◽  
Rat Pancreas ◽  
Number Ratio ◽  
A Cells

ABSTRACT Both types of pancreatic A cells were identified in the sheep, hamster, guinea pig, rat, pig and monkey. The argyrophil A1 cells displayed a distinct metachromatic reaction in the latter two mammals. While neither the A1 nor the A2 cells were localized to any particular islet region in the guinea pig and monkey, characteristic islet positions were noted in each of the other four species. There was a considerable increase of the A2/A1 cell number ratio with increasing islet diameter. The increased proportion of the A2 cells in the large islets was especially marked in the rat. While no differences were encountered between the duodenal and splenic pancreatic regions for the relative contributions of the A1 and A2 cells in the islets of the pig, monkey and guinea pig, the analyses of the rat pancreas revealed a higher frequency of A1 cells in the splenic part.

Preparation of Human Plasminogen Suitable as Substrate for Quantitative Determination of Plasminogen Activators

1966 ◽  
Vol 15 (03/04) ◽  
pp. 511-518
Author(s):  
W Berg ◽  
K Korsan-Bengtsen ◽  
J Ygge
Keyword(s):  
Ionic Strength ◽  
Quantitative Determination ◽  
Spontaneous Activity ◽  
Human Plasma ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
Simple Method ◽  
Neutral Ph ◽  
Human Plasminogen

SummaryA simple method for preparation of plasminogen with low spontaneous activity and soluble at a neutral pH and at physiological ionic strength is described. Euglobulin made from fresh, oxalated, BaSO4-adsorbed, human plasma was first purified by means of gel filtration on Sephadex G-200. After gel filtration, further purification and concentration was done on DEAE-sephadex A-50. The activity was 100-130 casein units per mg tyrosine.

scholarly journals The multiple forms of α-D-mannosidase in human plasma

1979 ◽  
Vol 179 (3) ◽  
pp. 583-592 ◽  
Author(s):  
S Hirani ◽  
B Winchester
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
Concanavalin A ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Exchange Chromatography ◽  
The Other ◽  
Multiple Forms ◽  
Simple Correlation ◽  
Multiple Components

The acidic alpha-D-mannosidase in human plasma closely resembles liver acidic alpha-D-mannosidase in its affinity for concanavalin A-Sepharose, molecular weight and resolution into multiple components on DEAE-cellulose. A combination of chromatography on concanavalin A-Sepharose and gel filtration on Sephadex G-200 and Sepharose 6B suggests that four forms of intermediate alpha-D-mannosidase, which differ either in their molecular weight of affinity for concanavalin A, exist in human plasma. A practical classification and nomenclature for the multiple forms of intermediate alpha-D-mannosidase in plasma based on molecular weight and affinity for concanavalin A is proposed. Multiple forms of intermediate alpha-D-mannosidase were also observed by ion-exchange chromatography on DEAE-cellulose, but there was not a simple correlation between these forms and those obtained with the other separation procedures. The form of intermediate alpha-D-mannosidase least abundant in plasma, approx. 7% of the activity, has very similar properties to the neutral alpha-D-mannosidase in human liver. In contrast, the other three forms of intermediate alpha-D-mannosidase, which account for over 90% of the activity, do not appear to be present in liver, except perhaps in trace amounts.

scholarly journals DISTRIBUTION, INHERITANCE, AND PROPERTIES OF AN ANTIGEN, MUB1, AND ITS RELATION TO HEMOLYTIC COMPLEMENT

1964 ◽  
Vol 120 (5) ◽  
pp. 897-924 ◽  
Author(s):  
B. Cinader ◽  
S. Dubiski ◽  
A. C. Wardlaw
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Gamma Globulin ◽  
Inbred Mice ◽  
Mammalian Species ◽  
Gel Filtration ◽  
Male Mice ◽  
High Concentration ◽  
Female Mice ◽  
Complement Level

An antigen, MuB1, present in the sera of some mice, can elicit a precipitating antibody in certain other strains of mice. An antibody to the antigen MuB1 can also be elicited in rabbits. 99 strains and substrains of inbred mice were tested for the presence of MuB1; the antigen was found in the sera of 44 strains (61 per cent) and 14 DBA substrains (52 per cent). Evidence is presented indicating that mice lacking MuB1 do not make a modified antigen, corresponding to MuB1, but are genetically deficient in synthetic ability at this site. By reaction with antibody to MuB1 an antigen corresponding to MuB1 was found in 13 of the 15 orders of mammals, and in 63 of 85 mammalian species tested, including man and guinea pig. The quantity of the antigen MuB1 is always greater in the serum of male than in the serum of female mice. The concentration of MuB1 increases with age; this increase is more marked in male than in female mice. By means of backcross experiments it was shown that the inheritance of MuB1 is unifactorial, is independent of the inheritance of the gamma globulin allotype MuA2, and is qualitatively independent of the sex of the parents. The antigen MuB1 is found in the euglobulin fraction of serum; it loses its ability to precipitate with antibody after heating at 56°C, but not after treatment with ammonia or hydrazine. By gel filtration, MuB1 is separated with a fraction containing molecules of molecular weight ≈ 150,000. An empirical correlation was observed between the presence or absence of MuB1 in the sera from inbred mice and the presence or absence of hemolytic complement (Hc), as measured by a test using a high concentration of rabbit hemolysin. In backcross experiments also, a correlation between hemolytic complement and the presence of MuB1 was demonstrated. As with MuB1, male mice had a higher hemolytic complement level than females. The particular component of complement which may be identical with MuB1 has not been identified.

Separation of Plasminogen Activators from Human Plasma and a Comparison with Activators from Human Uterine Tissue and Urine

1979 ◽  
Vol 41 (04) ◽  
pp. 734-744 ◽  
Author(s):  
Preben Kok
Keyword(s):  
Human Plasma ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
Particle Sizes ◽  
Uterine Tissue ◽  
Porcine Tissue ◽  
Normal Human ◽  
Molecular Sizes ◽  
Urokinase Plasminogen Activators ◽  
Acid Stable

SummaryNormal human plasma contains acid-stable as well as labile plasminogen activators. The activity of activators in plasma euglobulins was inhibited by EACA in an uniform pattern, similar to that obtained with the major activators in human uterine tissue or with the purified porcine tissue activator, but different from the patterns obtained with plasmin or with urokinase.Gel filtration at high ionic strength separated activators corresponding to particle sizes of 60,000 dalton and about 10,000 dalton, corresponding to two activators similarly obtained from human tissue. The 60,000 dalton activator was precipitated in the euglobulin fraction. Its concentration increased in plasma after exercise. The 10,000 dalton activator was found mainly in the supernatant. Gel filtration in 0.15 M solutions yielded activators in fractions of molecular sizes of 100-140,000 dalton and 200,000 dalton or larger.The activity of normal and exercise euglobulins was inhibited by antiserum to a plasminogen activator prepared from porcine tissue, but it was not inhibited by antiserum to urokinase. Plasminogen activators in human plasma euglobulins resembled immunochemi- cally the activators in human uterine tissue.

scholarly journals THE DERIVATION OF TWO DISTINCT ANAPHYLATOXIN ACTIVITIES FROM THE THIRD AND FIFTH COMPONENTS OF HUMAN COMPLEMENT

1968 ◽  
Vol 127 (2) ◽  
pp. 371-386 ◽  
Author(s):  
C. G. Cochrane ◽  
H. J. Müller-Eberhard
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Gel Filtration ◽  
The Other ◽  
Human Complement ◽  
Guinea Pig Ileum ◽  
Venom Protein ◽  
Similar Activity ◽  
Pig Skin ◽  
The Third

Anaphylatoxin activity was derived from both human C'5 and C'3 molecules. This was achieved in the case of C'5 by interaction with trypsin or with EAC'4, oxy2a, 3. The smooth muscle-contracting material obtained from the treated C'5 was found to be a fragment of approximately 9,000–11,000 molecular weight. Its action was inhibited with antihistamine. The trypsinized C'5 also increased vascular permeability in guinea pig skin. When human C'3 was incubated with C'3 inactivator complex, which consists of a cobra venom protein and a ß-globulin of human serum, anaphylatoxin activity was observed. The activity was associated with a fragment cleaved from the C'3 molecule, having a molecular weight of between 6,000 and 15,000 as determined by gel filtration techniques. Similar activity was derived from C'3 by the C'3-converting enzyme in free or in cell-bound form. The C'5 anaphylatoxin failed to cross-desensitize guinea pig ileum to the contracting capacities of C'3 and guinea pig anaphylatoxin and vice versa. Anaphylatoxin prepared from C'3 by all methods mentioned above caused cross-desensitization to the other C'3 derivatives, but failed to desensitize to guinea pig anaphylatoxin.

Separation of Plasminogen Activators from Human Uterine Tissue and a Comparison with Activators from Human Urine and Porcine Tissue

1979 ◽  
Vol 41 (04) ◽  
pp. 718-733 ◽  
Author(s):  
Preben Kok
Keyword(s):  
Plasminogen Activator ◽  
Human Urine ◽  
Gel Filtration ◽  
Ammonium Thiocyanate ◽  
Plasminogen Activators ◽  
Particle Sizes ◽  
Uterine Tissue ◽  
Porcine Tissue ◽  
Major Activity ◽  
Proliferative Phase

SummaryThree types of plasminogen activator could be distinguished in extracts from human uterine tissue. The activators differed in thermostability or in mode of inhibition by EACA.All the extracts contained stable as well as labile activators. The saline extracts were uniformly inhibited by increasing concentrations of EACA. Extracts made with 2 M ammonium thiocyanate were either uniformly inhibited by EACA or showed deflections indicating contamination with an activator, which was inhibited in a biphasic manner. It was possible to distinguish between: (1) An activator, abundantly present in the tissue, which was uniformly inhibited and stable. (2) Another uniformly inhibited activator, which was labile. (3) An activator, inhibited in a biphasic manner, similar to urokinase, which was present in varying amounts in uteri with the endometrium in the proliferative phase.Gel filtration of the uterine extracts showed two major activity peaks corresponding to particle sizes of 60,000 dalton and about 10,000 dalton.Antiserum to purified plasminogen activator, prepared from porcine ovaries, inhibited the activity of the human uterine extracts, but not the activities of human urokinase or urine. Urokinase antiserum in a concentration completely inhibiting human urine or urokinase, inhibited only 10% or less of the activities of human uterine extracts.

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