Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.2.1.36 (hyaluronidase)
4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An investigation was conducted on the effect of formocresol treatment of the aqueous extractability and enzymatic susceptibility of excised implant tissue. The treated tissue demonstrated a decreased solubility and a diminished digestibility by trypsin, pepsin and collagenase. However, its reactivity toward hyaluronidase showed little alteration.
...
PMID:The effects of formocresol on rat sponge implant tissue: a biochemical study. 20 Jun 37

Calf pulp was treated with full-strength formocresol, diluted formocresol, or saline for 4 hours. After washing and homogenization, the water extractable supernates were analyzed for total amino acid, carbohydrate, and hydroxyproline content. Additional samples were tested against trypsin, pepsin, collagenase, and hyaluronidase. Other tissue samples treated with 1/5, 1/10, and 1/25 dilutions of formocresol were subjected to trypsin and collagenase. The control tissue gave 50 per cent more extractable material, which contained over 300 per cent more total amino acids and hydroxyproline but only slightly more carbohydrate than the treated tissue. Formocresol treatment produced an 80 to 90 per cent reduction in reactivity to trypsin, pepsin, and collagenase but little change from hyaluronidase action. The increase in reactivity of the tissue to enzyme hydrolysis paralleled the increase in dilution of formocresol. These results indicate a profound effect on the protein fraction of pulp exposed to full-strength formocresol.
...
PMID:Biochemical effects of formocresol on bovine pulp tissue. 20 81

Kidney cells of the marine stickleback Spinachia have been studied with histochemical methods for the demonstration of glycoconjugates. The fine structure of epithelial cells is described. Mucus threads in the nephronic tubule of sexually mature consist of neutral glycoprotein which corresponds with the secretory granules in proximal tubule segment II cells. Large lysosome-like inclusions, which also react with PAS, are present in many P II cells. All cells of the collecting duct epithelium differentiate into mucous cells in male Spinachia. The nature of their secretory products, which are well preserved by freeze-drying, is discussed. Sialylated glycoprotein is present in mucus granules and sulphated glycoprotein can be demonstrated at the apex of collecting duct cells. Collecting duct cell mucus can be digested with testicular hyaluronidase indicating that proteoglycans may be involved in the structure of macromolecules. The observations are compared with studies of mucus production in the urinary apparatus of several other vertebrates.
...
PMID:The kidney of a teleost, Spinachia spinachia. II. Histochemical identification of sialic acid-containing glycoprotein and fine structure of mucus secreting cells. 58 60

The chorionic villi of placentas, 10 to 40 weeks of gestation, were examined for A and B blood group antigens with an immunoferritin technique. No specific ferritin attachment was shown on the plasma membrane of the villous trophoblasts. Furthermore, after trophoblast cell-surface mucosubstances (perhaps the barrier of the placental antigenicity, according to some authors) were digested with several enzymes, such as neuraminidase, hyaluronidase, chondroitinase ABC, pepsin, trypsin, and pronase, no ferritin tagging was observed on the plasma membrane of the villous trophoblasts. We have concluded that our failure to detect the A and B blood group antigens was not due to the masking of antigens by mucosubstance coating the trophoblasts, but was due to the intrinsic deficit of those antigens in the plasma membrane of the human trophoblasts.
...
PMID:Innumoelectron microscopy of the human chorionic villus in search of blood group A and B antigens. 79 65

The release of beta-lysin, which followed the intravenous injection of antigen-antibody complexes, did not take place when these complexes were added to citrated whole blood but did occur in heparinized blood. beta-Lysin release in heparinized blood was inhibited by citrate but were reversed by the addition of calcium ions that implicated complement reactions. Fourteen different enzymes were added to platelet-rich plasma (PRP). Streptokinase, neuraminidase, papain, phospholipase C, sulfatase, and trypsin caused platelets to release significant quantities of beta-lysin, whereas elastase, phosphatase, protease, ribonuclease A, hyaluronidase, lipase, and pepsin caused little or no increase in the plasma beta-lysin concentration. One enzyme, fibrinolysin, inactivated beta-lysin faster than it was released. The enzyme-induced release of beta-lysin from PRP was often accompanied by a reduction in the number of platelets. The intravenous injection of streptokinase, neuraminidase, and sulfatase caused in vivo releases of beta-lysin into the plasma. The platelet-aggregating substances collagen, arachidonic acid, and adenosine 5'-diphosphate caused beta-lysin to be released from PRP. The platelet-aggregating substances L-epinephrine, zymosan, fibrinogen, reserpine, and serotonin caused little or no release of beta-lysin from platelets. The results of this study indicate that the release of beta-lysin during antigen-antibody-complement reactions, blood coagulation, phagocytosis, and inflammation could be enzyme mediated.
...
PMID:Release of beta-lysin from platelets caused by antigen-antibody complexes, purified enzymes, and platelet-aggregating substances. 84 4

A series of monoclonal antibodies was prepared against the pepsin-resistant fragment of type IX collagen designated HMW. One of these antibodies (called 2C2) was selected for further analysis. Antibody 2C2 showed no cross-reactivity with other collagen types by inhibition enzyme-linked immunosorbent assays. It recognized an epitope present in native HMW, but failed to recognize any of the three chains of HMW fractionated after denaturation followed by reduction and alkylation of interchain disulfide bridges. Electron microscopic observations after rotary shadowing showed that the location of the epitope for antibody 2C2 was close to the carboxy-terminus of HMW. Immunofluorescent staining of sections of embryonic and adult cartilage with antibody 2C2 after removal of proteoglycans by testicular hyaluronidase digestion showed that type IX collagen is distributed throughout the cartilage matrix, and is not present in other connective tissues or skeletal muscle. The intact type IX collagen molecule, which was secreted by a suspension culture of freshly isolated embryonic chick chondrocytes, was recognized by rotary shadowing in the presence of antibody 2C2 after first precipitating the procollagens from the culture medium with ammonium sulfate (30%). Two different collagenous molecules were present in the precipitate: a longer molecule of type II procollagen (average length, 335 nm) with both amino- and carboxy-propeptides still remaining uncleaved, and a shorter molecule (average length, 190 nm) which was identified as type IX collagen. Antibody 2C2 consistently bound to the shorter molecules at a site located 136 nm from a distinctive knob at one end of the molecule, and did not bind to any specific site on the type II procollagen molecules. The structure of the intact type IX collagen molecule with the location of both collagenous and noncollagenous domains was as predicted after converting the nucleotide sequence of a cDNA clone encoding for one of the chains of type IX collagen to an amino acid sequence (Ninomiya, Y., and B. R. Olsen, 1984, Proc. Natl. Acad. Sci. USA, 81:3014-3018).
...
PMID:Monoclonal antibody against chicken type IX collagen: preparation, characterization, and recognition of the intact form of type IX collagen secreted by chondrocytes. 241 37

Monoclonal antibodies were prepared against the pepsin-resistant fragments (X1-X3) of bovine type IX collagen. One of the five hybridomas that gave a positive reaction in an enzyme-linked immunosorbent assay was selected (H1a) for structural analysis and immunolocalization of type IX collagen. The location of the epitope for H1a was deducted from immunoblots and electron microscopic observations after rotary shadowing. The H1a antibody binds to one end of the longest X2, X3, X4 molecules, and preferentially 40-55nm from one end of X1 molecules thus, on or near the noncollagenous domain, NC2. Different immunolocalizations of type IX collagen in the superficial, middle and deep zones of fetal calf epiphyseal cartilage were observed depending on the thickness of the section and on hyaluronidase digestion conditions. In the middle and deep zones, staining with H1a throughout the matrix was obtained only with thin sections (5 microns) and digestion for 1 h at 37 degrees C. With thick sections (15 microns) or with digestion for 1 h at 24 degrees C, staining was restricted to the pericellular regions. Staining throughout the matrix was obtained in the superficial zone under all experimental conditions. Without hyaluronidase treatment, no immunofluorescent staining was seen with either H1a or polyclonal antibody to type II collagen, indicating that type IX collagen is present throughout the matrix in the different zones of fetal calf cartilage. This result is in good accordance with the recent demonstration of common cross-links between type II and type IX collagen in chicken and bovine cartilage. However, the preferential unmasking of type IX collagen antigenic sites in the pericellular regions of middle and deep zones of fetal calf cartilage does not preclude the presence in that region of a special pericellular organization of the collagenous network.
...
PMID:Problems in the immunolocalization of type IX collagen in fetal calf cartilage using a monoclonal antibody. 247 27

We have shown that pepsin 1 can be prepared in milligram quantities from human gastric juice by semi-preparative high-performance ion-exchange chromatography. Further investigation into the elution of this enzyme using linear chloride gradients have shown it to be a heterogeneous mixture, the components of which all have peptic activity, but differing specific activities. These components are changed in number and retention time by incubation with hyaluronidase and aryl sulphatase, but not by neuraminidase or acid phosphatase, implying the presence of a sulphated proteoglycan.
...
PMID:Heterogeneity of human pepsin 1, as shown by high-performance ion-exchange chromatography. 250 11

Benign and malignant fibrous histiocytomas are composed of an admixture of fibroblast-like and histiocyte-like cells and of a changing amount of fibre structures which tend to be arranged in a so-called storiform pattern. In order to study the organization of the extracellular matrix, the distribution of fibronectin was investigated immunohistochemically. Using the PAP technique and the indirect immunofluorescence method, paraffin sections of formaldehyde fixed tissue specimens of 25 tumours (12 benign fibrous histiocytomas, 12 malignant fibrous histiocytomas, and 1 atypical fibroxanthoma) were studied. A pretreatment with hyaluronidase and proteolytic enzymes (trypsin, pronase, pepsin) was performed to unmask the antigen. Best results were obtained with pronase E or, sometimes even better, by employing a combination of pronase E and hyaluronidase. Generally fibronectin could be demonstrated in the matrix substances of fibrohistiocytic tumours, but the immunohistochemical staining patterns of benign and malignant tumours differed. In benign fibrous histiocytomas, a regular distribution of fibronectin was found in cellular areas. Parallel to formation of collagen fibres, the reaction decreased and in dermatofibromas showing abundant hyalinized collagen the staining proved to be quite weak. In malignant fibrous histiocytomas, the immunostaining was very irregular. In cellular areas consisting of spindle cells, an intense reaction could be observed. Tumours with storiform or fascicular fields exhibit a delicate network of fibronectin encircling individual fibroblast-like cells. In the course of fibre formation, the matrix staining for fibronectin revealed a distribution similar but not identical with that obtained with the reticulin stain. Simultaneous to the occurrence of collagen fibre bundles, fibronectin decreased and in areas of hyalinization the staining was considerably diminished. In areas of undifferentiated small cells, in myxoid zones as well as foci of xanthoma cells, and in pleomorphic portions the immunostain was negative. The distribution in atypical fibroxanthoma is similar to that observed in storiform and pleomorphic variants of malignant fibrous histiocytomas. The results support the suggestion that fibronectin is the first sign of the typical basic pattern of fibrohistiocytic tumours preceding the formation of reticulin and collagen fibres. The expression of fibronectin on cell surfaces as well as in intercellular matrix may be closely related to the organization of the growth patterns of fibrohistiocytic tumours.
...
PMID:Fibronectin in relation to growth patterns of fibrohistiocytic tumours--an immunohistochemical study of benign and malignant fibrous histiocytomas. 282 24

Pepsinogen has previously been shown to bind non-specifically to immune complexes and aggregated immunoglobulins. We demonstrate here using a solid-phase immunoassay that immunoglobulins aggregated by heat or glutaraldehyde bind non-specifically to several different enzymes. Some of these, including pepsinogen (marketed as pepsin), hyaluronidase and trypsin, are used in the breakdown of tissues or biochemical preparations during the preparation of antigens. Contamination of impure antigens by enzyme is likely to lead to products which bind non-specifically to immune complexes. This can cause misidentification of complexes as antibodies. We recommend that all tests for specific antibody involving the use of antigens prepared by these or other enzymes should include a control with aggregated immunoglobulin substituted for the test serum.
...
PMID:Binding of monomeric and aggregated immunoglobulin to enzymes. A source of artefact in antibody assays. 291 Oct 16


1 2 3 Next >>

---