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

An antigen was detected in pooled human nephroblastomas using antiserum prepared in rabbits against an ethylemediaminetetra acetic acid (EDTA) extract of the tumors. This antigen was not found in normal human plasma or kidney extracts, and was not related to the ABO or Forssman blood groups. The antigen was detected in extracts of cultured nephroblastoma cells, but was not present in extracts of normal human fetal kidney cell cultures. The antigen is believed to be present at the cell surface, as cell viability was not significantly lowered during the extraction procedure. A reaction of complete identity was demonstrated by Ouchterlony double diffusion experiments with this antigen and purified bovine fetuin. The antigen was not found in extracts of human fetal spleen, thymus or kidney, nor in human fetal serum. Furthermore, the antigen does not possess determinants in common with the human alpha-fetoprotein of hepatomas, nor was it detected in human renal clear cell carcinoma. Initial characterization of the antigen showed it to be nondialysable, not sedimentable at 100,000 times g for 2 h, stable to repeated freeze-thawing and to incubation at 56 degrees C for 1 h, and water soluble over a wide pH range. The antigen was susceptible to digestion with pronase and trypsin and possibly hyaluronidase, but not to ribonuclease or neuraminidase. The protein portion is therefore of major importance to the structural integrity of this antigen. The relationship between this antigen and other abnormal materials reported previously in nephroblastoma patients is being studied.
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PMID:A fetuin-like antigen from human nephroblastoma. 5 Feb 93

Human, guinea pig and rabbit skin homogenates were digested with trypsin and extracted with phenol water. Antisera were raised in guinea pigs and rabbits by immunization with extract recovered from the water phase (TPW extract). All sera showed increased titres in indirect haemagglutination tests. The results of absorption and inhibition experiments indicated antibodies against a common antigenic determinant. These antibodies also agglutinated erythrocytes sensitized with autologous antigen. In addition, serum from rabbits immunized with human or guinea pig skin extract contained antibodies against species-specific determinants. Rabbit antiserum precipitated guinea pig skin extract. The antigen involved had specificity identical with that of an antigen in the human, but not in the rabbit skin, extract. Oxidation of the human TPW extract with periodate destroyed the precipitinogen and the species-specific haemagglutinogen while the common determinant was not affected.
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PMID:Specificity of antigens in aqueous phenol extracts of skin examined by means of guinea pig and rabbit immune sera. 5 Oct 11

The immunological properties of water-soluble acid neurospecific antigens A and D of the bull brain were studied as affected by heating and proteolytical enzymes (trypsin, mixture of trypsin and alpha-chymotrypsin, protease from Streptomyces griseus). The immunological activity of antigen A is not changed essentially after its heating for 20 min at a temperature of 70-80 and 24-hour proteolysis with trypsin. Heating at 90-100 C as well as hydrolysis with protease from Streptomyces griseus and mixture of trypsin with alpha-chymotrypsin for the same time decrease the immunological activity of antigen A. The immunological activity of antigen A lowers after heating for 20 minutes at a temperature of 60 C and the action of all the studied proteolytical enzymes for 24 hours. The data obtained evidence for protein nature of antigens A and D.
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PMID:[Effect of temperature and proteolytic enzymes on the immunological properties of 2 acid neurospecific antigens]. 6 Aug 16

Homogenated stratum coreum, callus and psoriatic scales were extracted with (1) phenol water (PW) and (2) the combined use of trypsin digestion and phenol water extraction (TPW). The serological properties of the various preparations obtained were compared, using indirect haemagglutination, absorption and inhibition tests. The PW and TPW water phases contained two different antigens which were common to all three tissues. In addition, the periodate-treated TPW water phase of stratum corneum contained an erythrocyte-sensitizing antigenic determinant. This, however, cross-reacted with the untreated and periodate-treated preparation of psoriatic scales, whereas callus lacked the determinant present after treatment with periodate. Apparently callus and psoriatic scales lacked some components present in stratum corneum, but determinants specific for callus or psoriatic scales were not detected.
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PMID:Comparison of human stratum corneum, callus and psoriatic scales by means of serological methods. 6 92

Preparation of small vertebrates cleared after alcian blue staining of cartilage is facilitated by trypsin digestion. Specimens are fixed in formation, washed, skinned, and eviscerated. After staining in a solution of alcian blue in acetic acid-alcohol for 24-48 hours, they are transferred to water through graded alcohols. Excess alcian blue is removed over a period of up to three weeks by changes every 2-3 days of 1% trypsin in approximately one-third-saturated sodium borate. Bony tissues may be stained after this in a solution of alizarin red S in 0.5% KOH. Specimens are bleached if necessary and dehydrated through graded KOH-glycerine mixtures for storage in glycerine. Since alcohol treatment in addition to formalin fixation does not affect results with this method, it should be useful to researchers who want to study the cartilage or cartilaginous skeletons in museum specimens, which are routinely fixed in formalin and stored in alcohol.
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PMID:Enzyme clearing of alcian blue stained whole small vertebrates for demonstration of cartilage. 7 69

Differential staining of rat-like hamster chromosomes revealed: 1) C- and G-banding of chromosomes depending upon the Giemsa solvent (distilled H2O and phosphate buffer correspondingly) in case of ordinary staining; 2) dependence of C-banding pattern on the C-method; 3) different resistance of C-bands to trypsin action; 4) dependence of Q-bands on the fluorochroms employed (A, 33258 H, AO), the second non-fluorescent (A, 33258 H) near-centrometric heterochromatic region is brilliantly fluorescing when AO is employed; 5) heterogeneity of C-, G- and Q-bands, i.e. similarly stained region, may differ in their structural-functional peculiarities.
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PMID:[Heterochromatin of the rat-like hamster Tscherskia triton de Winton (Rodentia, Cricetinae), II]. 8 52

Interactions between native terrylytin and trypsin and their derivatives modified by water-soluble dextrans on one hand and human blood serum inhibitors on the other, were studied. It was shown that modification of the enzymes results in changes in the type of their inhibition by blood serum due to a decrease of affinity of polymeric enzyme forms for alpha 2-macroglobulin and alpha 1-antitrypsin. The inhibition constants for native and modified forms of terrylytin and trypsin were calculated. The effects of steric and electrostatic factors on the interaction between inhibitors of blood and polymeric forms of proteinases are discussed.
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PMID:[Interactions between human blood serum inhibitors and native and modified dextran proteinases--terrilytin and trypsin]. 8 89

Highly purified basic proteins have been isolated from bovine and turkey brains by a novel method employing acid-acetone extraction. The final product gave a single band on polyacrylamide gel electrophoresis at pH 4.3 and in the presence of sodium dodecyl sulfate. Both proteins have arginine at the COOH-terminus while the NH2-terminal residue cannot be detected and is probably blocked. A higher ratio of histidine to lysine and a greater proportion of serine and valine was found for the turkey compared with the bovine protein. Both proteins contain one tryptophan and two methionine residues. However, it was found from cyanogen bromide treatment that there is a marked difference in the location of one of the methionine residues, while the tryptophan-containing peptides liberated after trypsin digestion have different mobilities on peptide maps. When dissolved in water these proteins give a typical random coil curve from circular dichroism (CD), whereas in 80% methyl alcohol they assume a 25% alpha-helix.
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PMID:Characterization of turkey myelin basic protein isolated by a simple procedure. 9 40

It is known that the negatively stained preparations of inner mitochondrial membrane display characteristic approximately 9 nm F1 (ATPase) knobs projecting from the matrix surface. Freeze-etch studies have reported the absence of such knobs from the "etched" surface of the inner mitochondrial membranes. We have demonstrated their presence on the surface of SMP (submitochondrial particles) prepared by freeze-drying for transmission electron microscopy. This identification has been substantiated by comparison with freeze-dried TU particles (trypsin-urea treated SMP) that are devoid of F1 (ATPase). It has been suggested that a layer of water molecules is strongly adsorbed to the surface of SMP and does not sublime during normal freeze-"etching."
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PMID:Visualization of mitochondrial coupling factor F1(ATPase) by freeze-drying. 9 68

Earlier studies have shown that a substance(s) released from the egg jelly of the toad Bufo arenarum is required for fertilization. In this paper some properties of this diffusible factor were further examined, and a procedure was designed for its isolation from crude egg extracts. The active component is soluble in water and ethanol, and insoluble in chloroform, ether and n-butanol. The biological activity is stable to liophylization and to heat, and remains unaffected after trypsin treatment. In contrast, it is impaired after treatment with ethyl acetate, 0.1 N HCl or chloroform, and is completely destroyed after converting the diffusible factor into ash. Data are presented showing that the recovery of fertilizability of extracted eggs in the bioassay system as carried out under present conditions, cannot be ascribed to a pH alteration of the insemination medium. This lends further support to the view that diffusible factor activity is not mediated through a pH effect. The factor was purified by gel chromatography coupled with desalting and paper chromatography. The active molecule is of low molecular weight and appears associated with a high pH ninhydrin-positive fraction.
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PMID:Properties and isolation of the diffusible factor involved in Bufo arenarum fertilization. 11 83


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