{"title":"Friedländer synthesis of the food carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine.","authors":"S Lindström","doi":"10.3891/acta.chem.scand.49-0361","DOIUrl":"https://doi.org/10.3891/acta.chem.scand.49-0361","url":null,"abstract":"<p><p>2-Amino-1-methyl-6-phenylimidazo[4,5-b]pyridine has been prepared in 26% yield from 3-amino-2-phenylpropenal and creatinine which were heated with N,O-bis(trimethylsilyl)acetamide at 120 degrees C for 2 h. Under certain other conditions, the main product was a pyrimidine derivative.</p>","PeriodicalId":76966,"journal":{"name":"Acta chemica Scandinavica (Copenhagen, Denmark : 1989)","volume":"49 5","pages":"361-3"},"PeriodicalIF":0.0,"publicationDate":"1995-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18766803","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Facile desulfurization of cyclic thioureas by hydrogen peroxide in acetic acid.","authors":"S Grivas, E Ronne","doi":"10.3891/acta.chem.scand.49-0225","DOIUrl":"https://doi.org/10.3891/acta.chem.scand.49-0225","url":null,"abstract":"<p><p>A simple, mild and synthetically useful method for the desulfurization of cyclic thioureas and related compounds, existing as thiol-thione tautomeric mixtures, by hydrogen peroxide in acetic acid is proposed. The effect of substituting different solvents for the acetic acid was investigated.</p>","PeriodicalId":76966,"journal":{"name":"Acta chemica Scandinavica (Copenhagen, Denmark : 1989)","volume":"49 3","pages":"225-9"},"PeriodicalIF":0.0,"publicationDate":"1995-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18773899","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"An alternative synthesis of the NMDA antagonist CGS 19755 via free radical carbamoylation of ethyl isonicotinate.","authors":"I Martin, J Anvelt, L Vares, I Kühn, A Claesson","doi":"10.3891/acta.chem.scand.49-0230","DOIUrl":"https://doi.org/10.3891/acta.chem.scand.49-0230","url":null,"abstract":"<p><p>The NMDA antagonist CGS 19755 (cis-4-phosphonomethyl-2-piperidinecarboxylic acid) has been prepared by applying Minisci reaction conditions [formamide, hydrogen peroxide, iron(II) sulfate] to ethyl isonicotinate, reduction of the ester with sodium borohydride, alcoholysis of the 2-carboxamide, formation of 4-(diethylphosphonomethyl)-2-pyridinecarboxylate, hydrogenation of the pyridine nucleus, and acid hydrolysis. The overall, unoptimized yield was around 11%. The procedure employs cheap starting materials, is practical and avoids the use of toxic and hazardous cyanotrimethylsilane which is used in the published procedure.</p>","PeriodicalId":76966,"journal":{"name":"Acta chemica Scandinavica (Copenhagen, Denmark : 1989)","volume":"49 3","pages":"230-2"},"PeriodicalIF":0.0,"publicationDate":"1995-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18773900","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Purification and characterization of the bovine pituitary luteinizing hormone releasing hormone M(r) 60,000 binding protein.","authors":"J Christiansen, G Houen","doi":"10.3891/acta.chem.scand.48-0994","DOIUrl":"https://doi.org/10.3891/acta.chem.scand.48-0994","url":null,"abstract":"<p><p>Luteinizing hormone releasing hormone (LHRH) regulates the release of luteinizing hormone and follicle stimulating hormone from the pituitary. This process takes place through interaction with high affinity membrane receptors. In addition LHRH inhibits the growth of several cancer cell lines through the interaction with M(r) 60,000 LHRH receptors. Here we describe the purification to homogeneity of the M(r) 60,000 bovine pituitary LHRH binding protein in amounts allowing N-terminal sequencing and peptide mapping. The procedure describes solubilization of luteinizing hormone releasing hormone receptors from homogenized bovine pituitaries in an active form by using the detergent Triton X-114. The receptors were retained in the Triton X-114 phase during temperature-dependent phase separation. Preparative phase separations were performed directly on solubilized bovine pituitary extracts. SDS-PAGE of the purified LHRH receptor after LHRH-immobilized affinity chromatography showed the presence of a single band with M(r) 60,000. Partial sequencing of this band after trypsin digestion of gel pieces revealed unknown sequences with a possible homology to other receptors including some G-protein coupled receptors.</p>","PeriodicalId":76966,"journal":{"name":"Acta chemica Scandinavica (Copenhagen, Denmark : 1989)","volume":"48 12","pages":"994-1000"},"PeriodicalIF":0.0,"publicationDate":"1994-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18863450","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Human placental calreticulin: purification, characterization and association with other proteins.","authors":"G Houen, C Koch","doi":"10.3891/acta.chem.scand.48-0905","DOIUrl":"https://doi.org/10.3891/acta.chem.scand.48-0905","url":null,"abstract":"<p><p>Calreticulin is an intracellular protein known to be involved in calcium binding, but is also known to appear as an autoantigen in certain autoimmune diseases. The cDNA sequence is known but the protein has not yet been well characterized at the amino acid level. Owing to the possible involvement of this protein in autoimmune disease and with the aim of making monoclonal antibodies for use in assay development and immunohistochemistry, we have purified calreticulin using human placental material. Amino acid analysis of the purified protein confirmed the cDNA-derived composition, and only one discrepancy between the cDNA-predicted sequence and the amino acid sequence was found by peptide mapping and microsequencing. The protein contains one disulfide bridge and has one free SH group and the protein is neither glycosylated nor phosphorylated. Affinity chromatography of a placental protein extract on a column with immobilized calreticulin showed the existence of at least six proteins interacting with calreticulin. Using the purified calreticulin in Western blots, two out of eight patients with autoimmune disease diagnosed as having anti DNA antibodies in their serum were found also to contain autoantibodies to calreticulin in their serum.</p>","PeriodicalId":76966,"journal":{"name":"Acta chemica Scandinavica (Copenhagen, Denmark : 1989)","volume":"48 11","pages":"905-11"},"PeriodicalIF":0.0,"publicationDate":"1994-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18839437","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Erythrocyte lipid extraction in alcohol-chloroform systems: a comparative study.","authors":"W Q Wang, A Gustafson","doi":"10.3891/acta.chem.scand.48-0753","DOIUrl":"https://doi.org/10.3891/acta.chem.scand.48-0753","url":null,"abstract":"<p><p>Lipid extraction efficiency is variable when different methods are used on the same tissue. After a systematic comparison on erythrocytes, we found that this variability was due to several factors, such as the addition of alcohol and chloroform as a mixture, the use of repeated extractions or partition procedures after the extraction. Most important, however, was the uneven distribution of solvents and lipids in an apparently monophasic extraction system. This formation reduces lipid extraction and causes accumulation of lipids in the extract supernatant, which leads to an overestimation of the extracted lipid content. We recommend a one-step 18.75 volume of methanol-chloroform (1.5:1 v/v) method for lipid extraction from erythrocytes, with methanol added before chloroform. This method combines simplicity in the extraction procedure, complete extraction of cholesterol and total phospholipids, and reliability in the quantitation of the extracted lipids.</p>","PeriodicalId":76966,"journal":{"name":"Acta chemica Scandinavica (Copenhagen, Denmark : 1989)","volume":"48 9","pages":"753-8"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18942994","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Pigment interferes with cholesterol analysis in erythrocyte lipid extracts: a procedure for removal.","authors":"W Q Wang, A Gustafson","doi":"10.3891/acta.chem.scand.48-0699","DOIUrl":"https://doi.org/10.3891/acta.chem.scand.48-0699","url":null,"abstract":"<p><p>Removal of pigments from erythrocyte lipid extracts was achieved simply by adding isopropyl alcohol (2 ml) and silica gel H (0.05 g) to an aliquot of dried extract. This procedure is superior to other available methods because of its simplicity and high efficiency.</p>","PeriodicalId":76966,"journal":{"name":"Acta chemica Scandinavica (Copenhagen, Denmark : 1989)","volume":"48 8","pages":"699-700"},"PeriodicalIF":0.0,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18916614","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}