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

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The clinical, pathologic, and immunologic aspects of malignant lymphoma of centrocytic type (ML,cc) were studied at diagnosis and often at relapse in 18 patients. The typical patient was a middle-aged or older man with adenopathy, often massive splenomegaly, hepatomegaly, marrow involvement, and, not infrequently, peripheral blood involvement. Histopathologically, ML,cc had a diffuse or vaguely nodular growth pattern with, predominantly, cells resembling centrocytes (cleaved follicular center cells) sometimes with admixed small round lymphocytes but with virtually no transformed cells. In 2 cases the neoplastic cells formed a mantle zone around reactive-appearing follicles. Cell suspensions and frozen sections revealed the monoclonal B-cell nature of all but 1 nonmarking case, and the polyclonality of the follicles in the 1 mantle zone case tested. The B cells had some, but not all, characteristics of both normal mantle and follicular center cells when eight nodes were studied with the use of a panel of monoclonal antibodies, peanut lectin, and endogenous alkaline phosphatase activity. Of 13 patients who underwent repeat biopsies, 1 developed a high grade unclassifiable B-cell lymphoma, and 6 had less marked changes. None of 7 patients tested had a change in light chain class. In conclusion, ML,cc is a distinct entity separable from other B-cell lymphomas in which either centrocytes or small round lymphocytes predominate.
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PMID:Centrocytic lymphoma: a distinct clinicopathologic and immunologic entity. A multiparameter study of 18 cases at diagnosis and relapse. 641 75

Two major forms of human alpha-L-iduronidase have been individually purified over 175,000-fold to apparent homogeneity by sequential anion exchange, lectin affinity, and gel filtration chromatography. The two forms, initially designated as soluble and membrane-associated, were extracted from human lung in approximately equal amounts. Optimal solubilization of the membrane-associated form was facilitated by use of a non-ionic detergent or mannose 6-phosphate and saponin. Following detergent homogenization, the two forms were separated by anion exchange chromatography and then individually purified. The more electronegative form was membrane-associated, had a pI of approximately 5.9, and was selectively taken up (high uptake) by cultured Hurler syndrome fibroblasts; the more electropositive soluble form had a pI of about 6.6 and was incorporated into Hurler fibroblasts at a markedly lower rate (low uptake). After treatment with alkaline phosphatase, the pI values of both enzymes were about 7.8. Using 4-methylumbelliferyl-alpha-L-iduronide as substrate, the low and high uptake forms were each purified in milligram quantities to specific activities of 284,000 and 202,000 units/mg, respectively, with a combined yield greater than 35%. Each purified enzyme form migrated as a single protein band which also stained for enzymatic activity when electrophoresed in 7% native polyacrylamide disc gels at pH 4.3. By gel filtration, the high uptake form had an Mr = 85,000 whereas the Mr for the low uptake form was 68,000. Molecular weight estimates by analytical polyacrylamide gel electrophoresis were 82,000 and 70,000 for the high and low uptake forms, respectively. Rabbit anti-human low uptake alpha-L-iduronidase antibodies cross-reacted with the high uptake form as demonstrated by both immunotitration and Ouchterlony double immunodiffusion. Amino acid analysis revealed that the high uptake (higher molecular weight) form contained more arginine, glycine, alanine, glutamate or glutamine, leucine, isoleucine, histidine, and proline residues per molecule than the low uptake (lower molecular weight) form. Automated Edman degradation determined that the NH2-terminal residues of both forms were blocked. Both sodium dodecyl sulfate-polyacrylamide gel electrophoresis and high performance liquid chromatography demonstrated that each purified form was composed of several components; each post-high performance liquid chromatographic component retained catalytic activity and was immunologically cross-reactive with antibodies against the low uptake form.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Human alpha-L-iduronidase. I. Purification and properties of the high uptake (higher molecular weight) and the low uptake (processed) forms. 642 18

We describe two new methods for the separation and quantification of the bone and liver isoenzymes of alkaline phosphatase (EC 3.1.3.1) in plasma. In the first, we use wheat-germ lectin to precipitate the bone isoenzyme. About 80% of this, but minimal liver isoenzyme, is precipitated. The activity of the bone isoenzyme is calculated from measuring the alkaline phosphatase activity in the precipitate, that of liver alkaline phosphatase by subtracting the activity of the bone isoenzyme from total alkaline phosphatase activity. The liver fraction will also contain biliary, intestinal, and placental alkaline phosphatase if these are present in the original plasma, but correction for such activity is readily made. In the second method, samples are separated on cellulose acetate membranes that, before electrophoresis, have been soaked in buffer containing wheat-germ lectin. The bone isoenzyme is retarded and clearly separated from the liver fraction, allowing these isoenzymes to be quantified by densitometry. Both methods are rapid, reproducible, and suitable for use in the diagnostic laboratory.
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PMID:Two new methods for separating and quantifying bone and liver alkaline phosphatase isoenzymes in plasma. 654 74

M cells in Peyer's patch follicle epithelium endocytose and transport luminal materials to intraepithelial lymphocytes. We examined (1) enzymatic characteristics of the epithelium covering mouse and rat Peyer's patches by using cytochemical techniques, (2) distribution of lectin-binding sites by peroxidase-labeled lectins, and (3) anionic site distribution by using cationized ferritin to develop a profile of M cell surface properties. Alkaline phosphatase activity resulted in deposits of dense reaction product over follicle surfaces but was markedly reduced over M cells, unlike esterase which formed equivalent or greater product over M cells. Concanavalin A, ricinus communis agglutinin, wheat germ agglutinin and peanut agglutinin reacted equally with M cells and with surrounding enterocytes over follicle surfaces. Cationized ferritin distributed in a random fashion along microvillus membranes of both M cells and enterocytes, indicating equivalent anionic site distribution. Staining for alkaline phosphatase activity provides a new approach for distinguishing M cells from enterocytes at the light microscopic level. Identical binding of lectins indicates that M cells and enterocytes share common glycoconjugates even though molecular groupings may differ. Lectin binding and anionic charge similarities of M cells and enterocytes may facilitate antigen sampling by M cells of particles and compounds that adhere to intestinal surfaces in non-Peyer's patch areas.
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PMID:Cytochemical analysis of alkaline phosphatase and esterase activities and of lectin-binding and anionic sites in rat and mouse Peyer's patch M cells. 665 Apr 35

Two fractions were isolated by continuous density gradient centrifugation from total particulate matter of rabbit sciatic nerves: a minor fraction, B, consisting of small-sized membrane fragments and a major fraction, C, of characteristic multilayered myelin figures, with maxima at 0.33 and 0.58 M-sucrose, respectively. In comparison with C, fraction B was enriched in CNPase and alkaline phosphatase activities and the P0, 23K and Z proteins, but was virtually devoid of basic protein. The glycoprotein composition of all fractions was examined with four fluorescein isothiocyanate-labelled lectins (WGA, Con A, RCA-60, U.E.). These revealed the presence of six glycoproteins in all fractions with similar lectin binding capacities and molecular weights ranging from 35,500 to 16,000, of which P0 was the predominant component. Material found on the heavy side of fraction C was characterized by the presence of a multitude of glycoproteins which bound variable proportions of the four different lectins, suggesting substantial variations in their carbohydrate moieties. Their absence from the central portion of fraction C points to a location other than that of compact PNS myelin.
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PMID:The glycoprotein composition of peripheral nervous system myelin subfractions. 679 Jun 71

Intraluminal injections of lectins, including concanavalin A (Con A), wheatgerm lectin, and soybean lectin, Con A-Sepharose 4B beads, calcium ionophore A23187 or peanut oil into the left uterine horns of mice on day 4 of pseudopregnancy induced the formation of deciduomata and significantly increased the weight and alkaline phosphatase activity of uterine tissue on day 7 of pseudopregnancy. In contrast, injections of these materials into the uterine horns of non-pseudopregnant mice that had not been previously mated failed to induce similar responses. Tranylcypromine blocked the decidual cell reaction artificially induced by lectins, calcium ionophore A23187 and peanut oil in pseudopregnant mice. However, uterine responses observed after individual and concurrent injections with indomethacin, iproniazid, propranolol or progesterone indicated that this deciduoma-blocking effect may not be solely related to the ability of tranylcypromine to inhibit prostacyclin biosynthesis but may also involve catecholamines and luteolytic prostaglandins which interfere with decidualization on day 4 and day 6 of pseudopregnancy, respectively. A role for prostaglandins and uterine beta-adrenergic receptors, however, was implicated in the induction of decidualization because both indomethacin and propranolol blocked the response to peanut oil. The results suggested that the embryonic signal responsible for the induction of the decidual cell reaction in mice may involve surface interactions between the embryo and uterine luminal epithelium resulting in a stimulation of the uterus via glycoprotein receptors. A role for calcium was implicated in this phenomenon.
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PMID:Lectins, calcium ionophore A23187 and peanut oil as deciduogenic agents in the uterus of pseudopregnant mice: effects of tranylcypromine, indomethacin, iproniazid and propranolol. 680 81

Three cell lines of mature T cell origin established from patients with cutaneous T cell lymphoma-leukemia (CTCL) have been found to be constitutive producers of TCGF (L-TCGF). Biologically active L-TCGF can also be eluted from the plasma membranes of these cells. We have compared the biologic and biochemical properties of L-TCGF and TCGF derived from normal lymphocytes (N-TCGF). L-TCGF and N-TCGF share similar biologic activity: both support long-term growth of T cells that have undergone prior lectin or antigen stimulation, and have no effect on unstimulated T cells. However, L-TCGF is a more acidic (pI 4.5 vs 6.5 to 8.0) molecule than N-TCGF and elutes from DEAE-Sepharose at higher salt concentration (0.2 M NaCl vs 0.07 to 0.1 M NaCl). In addition, these two factors display differing mobilities on gel filtration. Treatment of L-TCGF with neuraminidase or alkaline phosphatase does not alter its pI, indicating that enzymatically vulnerable sialic acid or phosphate groups are not involved in the variation. The nature and significance of this biochemical variant remain unknown.
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PMID:A biochemical variant of human T cell growth factor produced by a cutaneous T cell lymphoma cell line. 698 Sep 38

A human cell line has been established from a transplantable xenografted human testicular tumor, which, both in the original tumor and in the xenograft, exhibited the histological characteristics of an undifferentiated malignant teratoma (embryonal cell carcinoma). The cells in culture were undifferentiated by biochemical, morphological, and ultrastructural criteria, growing as small islands of cells that tended to form aggregates at high density. The cells showed some variation in chromosome number with 30 to 40% of the cells having a normal human karyotype. The cells expressed high levels of alkaline phosphatase, which by heat inactivation and inhibition studies was 40 to 50% placental type alkaline phosphatase. None of the cultures produced human chorionic gonadotrophin, alphafetoprotein, carcinoembryonic antigen, or fibronectin, although at high cell densities plasminogen activator could be detected at low levels. Cell surface studies showed that the cells shared antigens with the murine embryonal carcinoma cell line F9, expressed beta 2-microglobulin at very low and variable levels, and bound the lectin peanut agglutinin. These studies suggest that this cell line has some of the characteristics described for murine embryonal carcinoma cell lines.
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PMID:Characterization of a new human cell line derived from a xenografted embryonal carcinoma. 717 48

Purified human alkaline phosphatases were separated by lectin binding affinity to Wheat germ lectin-Sepharose, Concanavalin A-Sepharose and Lentil lectin-Sepharose into three isoenzymes: the placental, the intestinal and the liver-bone-kidney-type isoenzyme. Therefore, the carbohydrate chains of purified human alkaline phosphatases demonstrate the same isoenzyme classes than studies on structural, catalytical or immunological properties. The liver-bone-kidney-type isoenzyme shows a not yet described microheterogeneity on Concanavalin A and Lentil lectin. Thus, lectin binding affinity is a useful tool for the purification and separation of human alkaline phosphatase.
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PMID:Differentiation of human alkaline phosphatases by lectin binding affinity. 720 90

A method for the visualization of concanavalin A (Con A) binding sites by electron microscopy of glycol methacrylate sections is presented. This method, which is an application of the alkaline phosphatase-labeled Con A conjugate technique, solves the problems not only of limited penetration of chemicals into tissue blocks but also of injuries to tissue sections due to irritative reagents experienced in Con A-peroxidase staining. Glycol methacrylate sections are incubated successively with an alkaline phosphatase-labeled Con A solution and a lead citrate medium for the enzyme activity. Different kinds of tissues from adult rats have been used to test the method; tracheal cartilage, aorta and jejunum. The localization of Con A binding sites demonstrated by this method is consistent with the results of other published studies. Appropriate controls have been performed (ie., omission of the conjugated lectin, lectin plus its inhibitor) and these substantiate the specificity of the method.
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PMID:Ultrastructural visualization of concanavalin A binding sites using alkaline phosphatase-labeled Con A and ultrathin glycol methacrylate sections. 739 73


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