Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A new immunohistochemical assay was developed for the detection of human monoclonal antibody (HuMAb) bound to human biopsied tumor tissues. A murine anti-idiotype monoclonal antibody, alpha type, 18C6 (IgGl), was raised against an IgM HuMAb, L612, defining a tumor-associated ganglioside antigen (GM3) and used as a probe in a three step cell-binding assay (HuMAb + anti-id + biotinylated anti-mouse Ig). Anti-id 18C6 has an exclusive binding specificity for HuMAb L612, but does not interfere with the binding of L612 to antigen positive melanoma cell lines or to a purified antigen, GM3. The applicability of 18C6 in the three step cell-binding assay was tested first using a melanoma cell line, UCLASO-M12. L612 bound to M12 cells was specifically detected by 18C6 without any background reactivity in ELISA. When this assay was compared with the standard two-step cell-binding assay (HuMAb + peroxidase-conjugated anti-human IgM) using various cultured tumor cell lines, parallel reactivity was observed. The three-step cell-binding assay was then applied to various fresh-frozen human tumor sections. Positive reactivity was demonstrated on various histologic types of human tumor tissues: primary melanoma (10/10), metastatic melanoma (4/4), nevus (10/10), lung cancer (3/6), breast cancer (2/6), and colon cancer (1/1). Adjacent normal tissues were unstained. Control experiments included the cell-binding assay with L612 alone, 18C6 alone. L612 + unrelated mouse IgG, and unrelated IgM HuMAb (L72) + 18C6; but biotinylated anti-mouse IgG did not react with these control preparations. The results indicate that anti-id 18C6 is a highly specific probe to assess the expression of the ganglioside antigenic epitope recognized by the L612 HuMAb on biopsied human tumor tissues.
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PMID:Murine monoclonal anti-idiotype antibody (alpha) as a probe to detect human monoclonal antibody bound to human tumor tissues. 223 Jan 46

Direct evidence is presented in support of mechanism-based (suicide) inactivation of lactoperoxidase by thiocarbamide thyroid inhibitors. The turnover of 1-methylbenzimidazolidine-2-thione was demonstrated by identifying the inhibitor-derived products 1-methylbenzimidazole and bisulfite ion that are formed concurrent to enzyme inactivation. The turnover of a hydroperoxide cosubstrate, 5-phenyl-4-pentenyl hydroperoxide, was quantitated from formation of the corresponding alcohol during enzyme inactivation. A specific inactivation pathway is suggested by the covalent binding of 1 mol of 14C- and 35S-labeled benzimidazolidine-2-thione and 1-methylbenzimidazolidine-2-thione per mole of inactivated lactoperoxidase. These results are explained by partitioning of inhibitor-derived S-oxygenated intermediates between turnover and inactivation pathways. The properties of the inactivation process are unique among thiono-sulfur compounds and suggest that benzimidazolinesulfenic acids are the reactive intermediates.
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PMID:Mechanism-based inhibition of lactoperoxidase by thiocarbamide goitrogens. Identification of turnover and inactivation pathways. 245 91

A retrograde tracing study in the mole using wheat germ-agglutinated horseradish peroxidase (WGA-HRP) indicated that the medial superior olivary nucleus (MSO) projects to the inferior colliculus (IC) bilaterally. Considering the strict ipsilateral projections from the MSO to the IC in all other eutherian species ever reported, the bilateral projection in the mole is quite unique. This may reflect specializations of the peripheral auditory apparatus of the underground dwellers and/or primitiveness of the insectivorous brains.
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PMID:Bilateral projections from the medial superior olivary nucleus to the inferior colliculus in the mole (Mogera robusta). 246 89

To study tumor-associated antigens that are immunogenic to humans, we have generated human monoclonal antibodies by fusing lymph node lymphocytes of a melanoma patient with a mouse myeloma cell line. We examined in detail the reactivity of one IgG antibody, termed 2-139-1. Immunostaining was performed with purified antibody conjugated to biotin. Binding was visualized by the avidin-biotin-peroxidase complex. With cultured cells, 2-139-1 stained 12 of 12 melanomas and 12 of 16 carcinomas. Reactivity was not detectable in seven neural crest tumors, six sarcomas, and 45 lymphomas and leukemias. This spectrum of reactivity was confirmed with sections of human tissues. The human monoclonal antibody 2-139-1 reacted against melanomas and not banal nevi. While the antibody reacted strongly to adenocarcinomas of the colon, prostate, rectum, and pancreas, it did not stain all the carcinomas tested. Furthermore, reactivity was not seen against sarcomas. Interestingly, 2-139-1 did not bind to the majority of the cells in normal tissues, including fetal tissues. The reactivity of 2-139-1 may be representative of the humoral immune response found in the regional lymph nodes of cancer patients. The distribution of this epitope in various tumors was fairly limited and appeared to be associated with malignant transformation.
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PMID:Tumor-reactive human immunoglobulin G monoclonal antibody from a melanoma patient. 247 81

Hypochlorous acid generated by myeloperoxidase reacts with histamine to produce chloramines. At pH 7, one mole of histamine monochloramine (HisCl) was generated per mole of H2O2 provided as substrate for myeloperoxidase. At pH 5, one mole of histamine dichloramine (HisCl2) was generated per two moles of H2O2. HisCl and HisCl2 had two and four oxidizing equivalents per molecule, respectively. In vitro, 30 microM HisCl and HisCl2 induced mepyramine-sensitive guinea pig lung parenchyma contraction with 89 and 56 percent of the response of an equivalent concentration of histamine. Pretreatment of lung strips with chloramines reduced the subsequent contractile response of the tissues to methacholine. These results suggest that H-1 histamine receptors provide for targeting of histamine chloramines to pulmonary tissue which may facilitate modification of tissue responses.
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PMID:Formation of chloramine derivatives of histamine: role of histamine chloramines in bronchoconstriction. 255 45

A light microscopic analysis of lectin receptors in normal placenta and trophoblastic disease was performed utilizing biotinylated Concanavalin-A (Con-A), wheat germ agglutinin (WGA), and peanut agglutinin (PNA), in conjunction with an avidin-biotin peroxidase complex. Hydatidiform mole, invasive mole and choriocarcinoma exhibited increased receptors to Con-A and WGA compared to normal placenta. Increased reactivity to Con-A and WGA was associated merely with increased growth and proliferation of trophoblasts rather than a malignant transformation. Normal placenta, partial and complete mole generally showed moderate to strong binding with PNA after neuraminidase treatment, while invasive mole and choriocarcinoma (11 of 15 cases) generally showed minimal to absent reaction with PNA. Heterogeneity of PNA binding in choriocarcinoma was manifested by the presence of PNA reactivity in the trophoblast membrane in 2 cases wherein no prior neuraminidase treatment was given. This suggests that in some malignant trophoblasts, there is absence of sialic acid in the terminal cell surface carbohydrate groups resulting in the exposure of N-acetylgalactoseamine.
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PMID:Lectin binding in tissues from hydatidiform mole, invasive mole and choriocarcinoma to concanavalin-A, wheat germ agglutinin and peanut agglutinin. 256 Mar 69

Numerical analysis of multiple binding of two ligands to one carrier has been accomplished, using the principle of several sets of acceptable binding constants, with bilirubin-laurate-albumin as an example. Binding of bilirubin to defatted human serum albumin was investigated by a spectroscopic method, based upon a difference of light absorption spectrum for free and bound bilirubin. The observations were supplemented with previous data from an independent technique, measurement of oxidation rates of free bilirubin with hydrogen peroxide and peroxidase. A continuous isotherm was obtained, showing binding of at least 4 mol bilirubin per mole albumin with the following stoichiometric binding constants, 1.11 X 10(8), 1.7 X 10(7), 8 X 10(5), and 4 X 10(4) M-1 at pH 8.2, ionic strength 0.15 M, 25 degrees C. The binding is anticooperative at all steps. A saturation level was not reached. Cobinding of bilirubin and laurate was studied, with up to 2 mol of each ligand per mole albumin, using the peroxidase method for determination of free equilibrium concentrations of bilirubin, and a dialysis rate technique for free laurate. The findings could be described in terms of a stoichiometric model. Heterotropic cooperativity was present among the first bilirubin and the first and second laurate molecules. More than two molecules of either ligand can be bound at the same time.
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PMID:Multiple binding of bilirubin to human serum albumin and cobinding with laurate. 282 43

The chloroperoxidase-catalyzed reactions of NAD(P)H with H2O2 in the presence of Cl- or Br- have been characterized. With 1 mol H2O2 per mol of NADH, one atom of 36Cl was incorporated into the 264-nm-absorbing intermediate product. This species was oxidized enzymatically by a second mole of H2O2 to a species distinct from NAD+, which retained one Cl atom. Spectroscopically identical species were also produced by reaction of NADH with one and two molar ratios of HOCl, respectively. These data indicate that, with respect to halogenation activities, chloroperoxidase functions similarly to myeloperoxidase, i.e., produces HOCl as the first product of Cl- oxidation by H2O2. Moreover, rapid chlorination of NAD(P)H followed by oxidation may be an important and highly lethal microbicidal effect of HOCl produced by myeloperoxidase in activated neutrophils.
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PMID:Chlorination of NADH: similarities of the HOCl-supported and chloroperoxidase-catalyzed reactions. 298 46

The catalase succinylation by succinic anhydride excess results in an almost complete dissociation of the enzyme into subunits possessing no catalase activity. The catalase subunits show the peroxidatic activity on o-dianisidine oxidation. The oxidation kinetics of this substrate by the succinylated enzyme was studied at various temperatures. The activation energy for this process is 10.1 kcal/mole. Within the temperature range of 31-65.5 degrees, the succinylated enzyme thermostability was studied by monitoring the peroxidatic activity decrease upon o-dianisidine oxidation. The activation energy for the succinylated catalase thermoinactivation equals to 15.5 kcal/mole. The peroxidatic activity of catalase subunits obtained by enzyme succinylation and acidic solution treatment was compared to that of horseradish peroxidase in the oxidation of the same substrate, i.e., o-dianisidine.
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PMID:[Peroxidase activity of succinylated catalase]. 299 61

By the peroxidase-antiperoxidase technique, the authors studied 7 malignant choroidal melanomas, 7 conjunctival nevi and 1 malignant conjunctival melanoma with the aim to detect the presence of vasoactive intestinal polypeptide (VIP), adrenocorticotropic hormone (ACTH), gastrin, estradiol and testosterone. Positive staining reaction for VIP, estradiol and testosterone was observed in both malignant melanomas of the choroid and conjunctival nevi. The case of conjunctival melanoma was positive for VIP and ACTH but not for estradiol and gastrin.
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PMID:Steroids and neuroendocrine hormones detected by the immunoperoxidase technique from malignant melanomas and nevi of the choroid and conjunctiva. 301 Feb 9


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