Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chromatin core particles, containing 140 base pairs (bp) of DNA plus the inner histones, can be nearly quantitatively formed either by reassociation from 2 M NaCl or by reconstitution from salt extracted histones and DNA. The reassociated or reconstituted particles appear to be identical with the native particles in all physical properties examined (sedimentation velocity, histone content, circular dichroism, and melting) as well as in their patterns of digestion by micrococcal nuclease, DNase I, and trypsin. In the presence of excess DNA, no "half-particles" are formed. In the presence of excess histone, aggregated structures are formed in addition to 11S core particles.
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PMID:Reconstitution of chromatin core particles. 92 32

In human deoxyhemoglobin a salt bridge links the alpha carboxyl of Arg-141 of each alpha chain to the epsilon-amino group of Lys-127 of the opposite alpha chain. These salt bridges are believed to contribute to the constraints in the quaternary deoxy (T) structure that lower its oxygen affinity. We have tested this hypothesis by incubating hemoglobin with 2 M hydrazine and trypsin which catalyzes specifically the reversible hydrazinolysis of the alpha carboxyl of Arg-141alpha. X-ray analysis shows the major structural difference between native deoxyhemoglobin and hydrazide deoxyhemoglobin to be the loss of the Arg-141alpha1-Lys-127alpha2 salt bridge and its Arg-141alpha2-Lys-127alpha1 counterpart. Accurate oxygen equilibrium curves of hydrazide hemoglobin show that blocking of the salt bridge has raised the oxygen affinity of the T structure while leaving that of the quaternary oxy (R) structure unchanged.
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PMID:Specific modification of the alpha chain C-terminal carboxyl group of hemoglobin by trypsin-catalyzed hydrazinolysis. 92 42

The differing sensitivities of the gallbladder and pancreas to graded doses of CCK have been claimed as important in normal digestive events. As both secretin and CCK are thought to be released in response to normal feeding, we have reexamined the sensitivities of the gallbladder and pancreas to graded increases of CCK with a constant secretin background. Under such conditions the increase in output of pancreatic trypsin and bile salt occurred simultaneously, the dose-response curves being almost superimposable. Thus, under conditions more closely approaching normal postcibal events, the previously described differing sensitivities of the pancreas and gallbladder were not observed.
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PMID:Similar sensitivities of pancreatic and biliary secretion to cholecystokinin plus secretin infusion. 95 77

Tryptic activity was competitively inhibited by cationic detergents which contain a cetyl group or longer hydrocarbon chains. Since the cetyl group is much longer than the side chains of lysine or arginine residues of substrates for trypsin, the nature of inhibition by cetyldimethylbenzylammonium chloride was examined using Na-benzoyl-L-arginine-p-nitroanilide as substrate and compared to that by butylamine. The inhibition by cetyldimethylbenzylammonium chloride occurred instantaneously and was completely reversible. The inhibitory effect of cetyldimethylbenzylammonium chloride was strongly dependent on both pH and salt concentration, contrasting with inhibition by butylamine which was relatively indifferent to these changes. The Ki value of cetyldimethylbenzylammonium chloride at pH 7.5 and 25 degrees C was calculated to be 2.0 +/- 0.3 mM, which is equal to that of butylamine within experimental errors. The standard entropy change of binding of cetyldimethylbenzylammonium chloride (44 +/- 2 cal/mol/degree) was much larger than for butylamine, indicating the formation of an efficient hydrophobic bond between the cetyl group and the enzyme.
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PMID:Interaction between proteins and detergents which contain a hydrocarbon chain longer than 16 carbon atoms. III. Competitive inhibition of trypsin by cetyldimethylbenzylammonium chloride. 95 49

A new method has been developed for the preparation of essentially pure primary cultures of neurons and non-neuronal cells from 11-day embryonic chick sympathetic ganglia. This method utilizes (1) differences in cell-to-substrate adhesiveness between neurons and non-neuronal cells and (2) the capacity of neurons to form homotypic aggragates. The maximum difference in adhesiveness between neuronal and non-neuronal cells occurred when the ganglia were dissociated with trypsin following collection in a salt solution lacking divalent cations. This difference allowed the preparation of highly purified non-neuronal cultures and 85-90% pure neuronal cultures. Intermittent agitation during the period of cell separation markedly increased the purity of the neuronal cultures by (1) inhibiting neuronal but not non-neuronal cell attachment and (2) facilitating the formation of homotypic neuronal aggregates in the supernatant. Neuronal and non-neuronal cultures prepared under these conditions were more than 99% pure on the basis of both morphological and biochemical analyses. Both cell types exhibited attachment efficiencies greater than 95% and have been maintained for several weeks in vitro. Thus, completely isolated neuronal and non-neuronal cultures can be prepared and maintained for prolonged periods in the absence of cells of the other type.
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PMID:Preparation of pure neuronal and non-neuronal cultures from embryonic chick sympathetic ganglia: a new method based on both differential cell adhesiveness and the formation of homotypic neuronal aggregates. 95 63

1. High-affinity estrogen-binding sites can be solubilized from the liver chromatin of estrogenized chickens by treatment of the chromatin with 2 M KCL/5 M urea and fractionation on hydroxylapatite. Two estrogen-binding proteins are eluted from hydroxylapatite columns by 20mM phosphate (binding protein I) and 200mMphosphate (binding protein II), respectively. 2. The binding protein I is part of a non-histone protein fraction containing acid-soluble and insoluble proteins, whereas the binding protein II elutes together with high molecular weight nonhistone proteins containing acid insoluble proteins only. Both binding proteins exhibit the smae affinity for estradiol (Kd approximately 10(-9) M). 3. From chromatin of untreated chickens very small amounts of binding protein I (0.1 pmol/mg protein compared to 1.9 pmol/mg protein from estrogenized chickens) with the smae affinity for estradiol as that from estrogenized animals can be solubilized. Binding protein II is not detectable. 4. The "soluble nuclear estrogen receptor" extracted from crude liver nucleir of estrogenized chickens by 0.5 M KCL behaves on hydroxylapatite very similarly to salt/urea-dissociated chromatin with respect to the binding protein I. No binding protein II, however, can be demonstrated. 5. Chromatography of various preparations on Bio-Gel A-1.5 m indicates that the binding protein II is a residual chromatin fragment containing an unseparated binding protein-DNA complex, whereas the binding protein I represents the solubilized nucleic-acid-free chromosomal estrogen receptor. The "soluble nuclear receptor" and the binding protein I, however, are not identical with respect to their chromatographic behaviour on Bio-Gel A-1.5m, even though their estrogen binding entity remaining after trypsin treatment seems to be very similar.
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PMID:Solubilization of the chromatin-bound estrogen receptor from chicken liver and fractionation on hydroxylapatite. 96 52

The permeability of standard Soviet ultrafiltration membranes prepared from cellulose acetates was investigated with respect to biologically active substances (hemoglobin, trypsin, ribonuclease, vitamin B12, hydroxytetracycline) and inorganic salt (KH2PO4). The arrest of a substance by a membrane of a certain structure depended primarily on the size of the substance macromolecule in the solution. The filtration rate was related to the membrane type, pressure gradient and composition of the filtered solution. Potential use of the tested membranes is described.
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PMID:[Permeability of acetylcellulose ultrafiltration membranes with regard to biologically active substances]. 100 67

1. Mitochondria were isolated from developing endosperm of Ricinus communis and were fractionated into outer membrane and inner membrane. The relative purity of the two membrane fractions was determined by marker enzymes. The fractions were also examined by negative-stain electron microscopy. 2. Membrane fractions were sequentially extracted in the following way. (a) Suspension in 0.5M-potassium phosphate, pH7.1; (b)suspension in 0.1M-EDTA (disodium salt)/0.05M-potassium phosphate, pH7.1; (c) sonication in 0.05M-potassium phosphate, pH7.1;(d)sonication in aq. Triton X-100 (0.1%). The membranes were pelleted by centrifugation at 100 000g for 15 min, between each step. Agglutination activity in the extracts was investigated by using trypsin-treated rabbit erythrocytes. 3. The addition of lactose to inner mitochondrial membrane resulted in the solubilization of part of the lectin activity, indicating that the protein was attached to the membrane via its carbohydrate-binding site. Pretreatment of the membranes with lactose before tha usual extraction procedure showed that lactose could extract lectins that normally required more harsh treatment of the membrane for solubilization. 4. Lectins extracted from inner membranes were purified by affinity chromatography on agarose gel. Polyacrylamide-gel electrophoresis of purified samples in sodium dodecyl sulphate indicated that at least part of the lectin present in inner mitochondrial membrane was identical with the R. communis agglutinin of mol.wt. 120 000.
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PMID:Lectins as membrane components of mitochondria from Ricinus communis. 100 61

Acetic acid extracts of human term placenta have been fractionated by pH and salt precipitations and by exclusion chromatography on a Sephadex G-75 column. A partially purified fraction (F-II) possessing uterotropic activity in immature and young mice was obtained. This active fraction was submitted to the action of protein denaturating agents (heat, 8 M urea) and of specific proteolytic enzymes (trypsin, alpha-chymotrypsin and pronase). These treatments completely destroy the uterotropic activity showing that the active substance is of protein nature. The administration of F-II to spayed mice did not produce any increase in their uterine weight suggesting that the uterotropic activity would be due to stimulation of the female gonad.
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PMID:Chemical and biological characterization of an active substance of the human placenta. 105 46

Actin was isolated from erythrocyte ghosts. It is identical to muscle actin in its molecular weight, net charge, ability to polymerize into filaments with the double helical morphology, and its decoration with heavy meromyosin (HMM). when erythrocyte ghosts are incubated in 0.1 mM EDTA, actin and spectrin are solubilized. Spectrin has a larger molecular weight than muscle myosin. When salt is added to the EDTA extract, a branching filamentous polymer is formed. However, when muscle actin and the EDTA extract are mixed together in the presence of salt, the viscosity achieved is less than the viscosity of the solution if spectrin is omitted. Thus, spectrin seems to inhibit the polymerization of actin. If the actin is already polymerized, the addition of spectrin increases the viscosity of the solution, presumably by cross-linking the actin filaments. The addition of HMM of trypsin to erythrocyte ghosts results in filament formation in situ. These agents apparently act by detaching erythrocyte actin from spectrin, thereby allowing the polmerization of one or both proteins to occur. Since filaments are not present in untreated erythrocyte ghosts, we conclude that erythrocyte actin and spectrin associate to form an anastomosing network beneath the erythrocyte membrane. This network presumably functions in restricting the lateral movement of membrane-penetrating particles.
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PMID:Actin in erythrocyte ghosts and its association with spectrin. Evidence for a nonfilamentous form of these two molecules in situ. 109 5


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