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)

This report describes macromolecules that bind (des-aspartic acid1)-angiotensin II, the des aspartic acid1 derivative of angiotensin I, and several biologically active and inactive analogues of these polypeptides. The macromolecules were found in the plasma of approximately 2 per cent of ambulatory adults and hospitalized children and 32 per cent of the patients at two institutions for the mentally retarded. The binding properties of these macromolecules were studied by incubating with peptides labeled with 125iodine, and separating bound from free labeled peptide using small gel filtration columns. The peptide-binding macromolecules from several patients were compared. They showed very similar specificity for a group of arginyl peptides of the des-aspartyl1-angiotensin sequence. The plasma binders differed from one another in their optimum pH and their mobility in electrophoretic fields. Those with more acid pH optima displayed more rapid electrophoretic mobility. The binders fell into two classes based on apparent molecular weight, approximately 140,000 and 250,000. Those with the higher apparent molecular weight contained a large proportion of binder that could be precipitated with antiserum to human IgA. Kinetic measurements showed that the plasma binders were somewhat heterogeneous with respect to affinity for (des-asp1)-angiotensin, with apparent association constants ranging from 10(7) to 10(8) M-1. Binding activity was labile to heat, and to treatment with pepsin or trypsin. It was inhibited by calcium, protamine, streptomycin, and some other cationic compounds. The plasma peptide binder differed in specificity and molecular weight from soluble angiotensin-binding molecules extracted from tissues, and from properties expected of a receptor for angiotensin. These macromolecules may be useful reagents for measuring (des-asp1)-angiotensins. Their presence in plasma samples may interfere with angiotensin assays in some circumstances.
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PMID:Peptide-binding macromolecules in the blood of seriously ill or mentally retarded patients. 0 55

The myeloma IgA protein produced by plasmacytoma XRPC-25, was isolated by affinity chromatography on dinitrophenyllysine-Sepharose. The affinity constant of the intact protein or its Fab' toward 2,4-dinitrophenyl-L-lysine (Dnp) was found to be 2.6 X 10(5) M-1. In order to prepare an Fv fragment (Hochman, J., Inbar, D., and Givol, D. (1973), Biochemistry 12, 1130) from this protein, the heavy and light chains were separated and the light chain was digested with trypsin at pH 8.2 to yield half a light chain. This digest was reassociated with the heavy chain and the recombinant was digested with papain at pH 5.7. Fractionation of this digest on a Sephadex G-75 column and Dnp-lysine-Sepharose resulted in the isolation of an Fv fragment which possesses one binding site for Dnplysine (Ka = 2.0 X 10(5) M-1). The active Fv fragment has a molecular weight of 23,400 and is composed of two peptide chains, each having a molecular weight of approximately 12,000. The N-terminal residues of these chains are aspartic and glutamic acids, which are also N-terminal in the heavy and light chains, indicating that the Fv is composed of VL and VH.
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PMID:Preparation of Fv fragment from the mouse myeloma XRPC-25 immunoglobulin possessing anti-dinitrophenyl activity. 0 96

Using the sucrose haemolysis reaction of Hartmann & Jenkins (1966) as a basic model, the low ionic strength reaction (LISR) of human blood was studied to determine: (1) serum Ig uptake by RBC with saline elution and 125I-IgG uptake, and (2) complement fixation (CF) to RBC with lysis of PNH cells and C3H/C4 antiglobulin haemagglutination (AH) of normal cells. The saline eluates were found to contain IgG and IgM with traces of IgA; their pH optima for the uptake by RBC were 6.0 +/- 0.5, 5.5 +/- 0.5 and c 5.0 respectively. The ratio of bound IgG to IgM was linearly related to the uptake pH. Both C4 AH and lysis were found to be optimum at pH 6.0--7.5, whereas the maximum C3 AH was at pH 6.0 +/- 0.5. The LISR performed at a constant pH (6.1 +/- 0.1) showed that an increasing concentration of neuraminidase (VCN) used in pretreatment of RBC was associated with a decrease in both IgG uptake and CF activity. A maximum VCN effect reduced the Ig uptake to c 20% of normal and abolished almost all the CF activity. An impaired LISR to various degrees was also observed with RBC pretreated with ficin, papain, bromelin, trypsin or protamine, and RBC from two individuals of En(a-) type. Preincubation of serum at LIS with and without RBC resulted in respectively a 'complete' and partial consumption of C in the fluid phase. The latter was not enhanced or inhibited by the addition of VCN-treated RBC for preincubation. A hypothesis is proposed suggesting that in the LSR the Ig uptake by RBC is an electrostatic interaction of the oppositely charged RBC and Ig and the CF to RBC results from C activation by the cell-bound IgG and IgM. In addition, a pH-dependent inactivation of the cell-bound C3 in the LISR is demonstrated.
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PMID:The low ionic strength reaction of human blood: relationship between the binding of serum immunoglobulin and complement of red blood cells and surface charge of the cells. 3 28

In order to obtain structural information and to facilitate studies of the covalent structure of T-cell immunoglobulin, we have performed investigations of the peptide fragments of the heavy chain of this molecule, on a comparative basis, with heavy chains of serum immunoglobulins. T-cell immunoglobulin was isolated from 125I-labelled culture medium of monoclonal continuously cultured T-lymphoma cells by means of immunoadsorbents. Peptides were prepared from the purified 125I-labelled heavy chain by means of cleavage with cyanogen bromide or digestion with trypsin. We then resolved these peptides and compared them with those peptides derived from 131I-labelled murine mu, gamma and alpha chains separately and in mixed label experiments by means of polyacrylamide gel electrophoresis in sodium dodecyl sulfate containing buffers, 2 dimensional peptide mapping and ion exchange chromatography. The profiles of the radiolabelled peptides obtained from the T-lymphoma heavy chains were quite distinct from those of murine gamma chains but indicated a structural similarity to both mu and alpha chains, which share some common peptides. These results are consistent with the antigenic and physicochemical data available and suggest that T-cell immunoglobulin is a new isotype that shows similarities to IgA and IgM, but of which the precise nature of the constant region has yet to be delineated.
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PMID:Molecular properties of T-lymphoma immunoglobulin. II. Peptide composition of the heavy chain. 10 42

Vaginal washings from women attending a veneral disease clinic were examined for the presence of protease that cleaved IgA subclass 1 (IgA1). In a crude assay, vaginal washings cleaved [125I]IgA1 in 19 of 25 specimens from individuals from whom Neisseria gonorrhoeae were cultivated. Forty-six specimens from 104 women whose cultures were negative for N. gonorrhoeae also cleaved [125I]IgA1. Vaginal washings from six of six women with culture-proven gonorrhea cleaved [125I]IgA1 into low-molecular-weight components identical to those produced by partially purified IgA1-specific protease from gonococci. The hydrolysis of [125I]IgA1 by vaginal washings from women whose cultures were negative for N. gonorrhoeae yielded cleavage products that resembled those of trypsin or alpha-chymotrypsin. These findings indicate that gonococci residing in the female genital tract produce IgA1-specific protease that can be detected in the vaginal washings of infected women.
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PMID:Studies on gonococcus infection. XVII. IgA1-cleaving protease in vaginal washings from women with gonorrhea. 10 39

A survey was made on workers handling powdered drugs in a pharmaceutical factory. In this factory, two kinds of anti-inflammatory enzyme (bromelain and trypsin), one anti-inflammatory agent (flufenamic acid), one antispasmodic (flopropion) and two kinds of antibiotics (ampicillin and cephalexin) are mainly produced. Twenty four workers were examined by interviews and checked by Cornell Medical Index, and 18 of them complained of respiratory symptoms. These 18 workers were physically examined by skin scratch tests, pulmonary function tests and serum immunological tests. Among 24 workers, 9 handled powdered drugs (A group), 5 handled the same in the past and had already been transferred to other sections for their symptoms (B group), 3 engaged in the process of capsul-filling (C group) and 7 handled several times occasionally during one year (D group). Their average months spent in handling powdered drugs were, in the case of anti-inflammatory enzyme, A group 53.2, B group 66.2, and in the case of antibiotics, 5 workers in A group 24.0, 2 workers in B group 7.0, 3 workers in C group 25.7. Twenty workers complained of symptoms which were mainly irritation of mucosa including the respiratory system and itching of the skin while they were working, and accelerated nasal discharge, urticaria and asthma after working. Group A and group B were higher than group D in the rate of respiratory complaints in C.M.I. (p less than 0.001). Fourteen workers pointed out anti-inflammatory enzyme as a cause of main symptoms, 7 workers flufenamic acid, 3 workers flopropion, 4 workers antibiotics. Three workers who had past history of asthma or articular rheumatism had been transferred to other sections. Of 18 workers who were physically examined, 11 workers showed positive reactions to skin scratch tests with handling drugs. On 8 workers of them, some kinds of drugs which were pointed out as drugs causing main symptoms reacted positively. Numbers of workers with increased immunoglobin values were, IgE 3, IgM 2, IgA 4, IgM 2. Two workers showed decreased FVC and FEV (1.0 sec.) values in pulmonary function tests. The causes of the occupational allergic reaction in this factory are guessed as follows: 1) control of powdered materials was incomplete in the process of production, 2) various kinds of sensitizing drugs were handled by the same workers.
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PMID:[Some experiments on the allergic reaction among workers in a pharmaceutical factory (author's transl)]. 16 Apr 71

A solid-phase radioimmunoassay (RIA) has been developed for the detection of human rotavirus-specific IgA, IgG, and IgM antibodies. Nebraska calf diarrhea virus grown in LLC-MK2 cell cultures in the presence of trypsin was directly adsorbed onto polystyrene balls, and antibodies that attached to the virus-coated balls were detected by subsequent binding of 125I-labeled antibodies specific to human alpha, gamma or mu chains of human Iga, IgG, or IgM immunoglobulins. A total of 116 serum specimens from 58 adult patients were tested. Binding ratios between the positive and the negative serum varied between 5 and 15, occasionally being 20 or more in the IgA and IgG assays, but rarely exceeding 3 in the IgM assay. The RIA was found to be more sensitive in detecting antibodies to rotavirus than the complement fixation (CF) test, the RIA titers obtained being 50--100 times as high as the CF titers. The method described offers a possibility of evaluating the immune response to human rotavirus and of detecting recent infection.
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PMID:Solid-phase radioimmunoassay of IgA, IgG, and IgM antibodies to human rotavirus. 22 43

Parallel determinations were made, of 10 individual serum proteins and of proteins in the bronchial secretion obtained by aspiration from 8 subjects that did not show manifest bronchopulmonary disease. By application of the formula suggested by Deuschl and Johansson it was found that 37 percent of IgG, 84,5 percent of IgA, 48,9 percent of transferrins, 15,2 percent of alpha-1-anti-trypsin and 11,3 percent of ceruloplasmin present in the bronchial secretion are synthetised in the bronchial mucosa itself, while the rest occur as a result of diffusion from the blood. Acid alpha-1-glycoprotein and haptoglobin from the bronchial secretion originate in the blood. IgM was evidenced in the bronchial aspirate in only 3 subjects, and alpha-2 macroglobulin was not found in any of the subjects.
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PMID:[Studies of the proteins in normal bronchial secretion]. 22 41

Aberration of IgA-bearing B lymphocytes in patients with IgA nephropathy has been investigated. Twelve patients with IgA nephropathy demonstrated a marked increase of IgA-bearing lymphocytes in peripheral blood, while ten patients with chronic proliferative glomerulonephritis without mesangial deposition of IgA showed normal amounts of IgA-bearing lymphocytes. The increase of IgA-bearing lymphocytes reflected that of IgA-producing lymphocytes, since lymphocytes obtained from patients with IgA nephropathy restored a high percentage of IgA-bearing cells in vitro after treatment with trypsin. Quantitation of IgA-bearing lymphocytes in peripheral blood is a useful method for screening of patients with IgA nephropathy.
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PMID:Increase of IgA-bearing lymphocytes in peripheral blood from patients with IgA nephropathy. 31 81

The present study compares formalin-fixed, deparaffinized and trypsin-treated (DTT) renal tissue sections with frozen sections for detecting immune complex deposition. Both DTT and frozen sections from 52 renal biopsies were stained directly with fluorescein isothiocyanate-conjugated antihuman IgG, IgM, IgA, fibrinogen, and C3. DTT sections alone were stained indirectly for C3 using a double conjugate technique. Antigen presence or absence on DTT section was accurately detected in 90 per cent of biopsies for immunoglobulins and fibrinogen and in 75 per cent for C3 when compared to frozen section. Furthermore, antigen deposition was found in 21 per cent of biopsies only on DTT sections (usually because frozen tissue lacked glomeruli). Frozen sections alone were treated with reagents of the fixation-embedding process and directly stained for IgM and C3 to determine antigen stability. Alkaline or neutral formalin pH helped maximize antigen preservation. DTT sections are a valuable tissue source for adjunctive diagnosis of renal disease.
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PMID:Immunofluorescence of deparaffinized, trypsin-treated renal tissues. Preservation of antigens as an adjunct to diagnosis of disease. 39 Feb 38


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