Z Skrzydlewski, R Rółkowski, K Worowski, A Piech-Brekin
{"title":"Complexoproductive and antiheparin properties of low density lipoproteins (LDL). II. Interaction of serum low density lipoproteins (LDL) with heparin of different molecular weight.","authors":"Z Skrzydlewski, R Rółkowski, K Worowski, A Piech-Brekin","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Quantity of unsoluble LDL complexes with heparin of different molecular weight in hypo-, normo-, and hyperlipemic blood serum in the presence of CaCl2 was estimated. At the same weight concentration the biggest quantity of LDL complexes are formed with heparin with heparin of the molecular weight 16000, the quantity is smaller with heparin of the molecular weight 5100, and it is the smallest with heparin of molecular weight 3700.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"32-7"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12510681","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":"Fibrin stabilizing factor activity of the skin carcinoma.","authors":"I Bernecka, A Klepacki, H Ostrowska","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Activity of fibrin stabilizing factor and contents of sulphydryl group in the homogenate of malignant skin carcinomas (melanoma, spinocellular carcinoma, basal cell carcinoma, fibromyoma, liposarcoma) is higher than in the homogenate of benign neoplasm (lipoma, papilloma) and in the homogenate of the normal skin. Fibrin stabilizing factor activity and contents of sulphydryl group in the blood serum of subjects with malignant skin carcinomas is slightly lower than in the blood serum of subjects benign neoplasm and in healthy subjects.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"3-7"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12461043","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":"AMP deaminase from porcine blood platelets, regulation by adenine nucleotides, phosphate and by Na+ and K+ ions.","authors":"M Tomasiak","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Porcine blood platelets contain a relatively high amount of AMP deaminase (14.4 U per 10 11 cells). The enzyme showed sigmoidal behaviour as a function of AMP concentration with a S0.5 value (substrate concentration required for half-maximum velocity) of 3.6 and 4.0 mM in the presence of Na+ and K+ respectively. MgATP and MgADP at micromolar concentration activated the enzyme. Activation by saturating MgATP and MgADP in the presence of Na+ or K+ converted the rate versus substrate plots to hyperbolic with a dramatic decrease of S0.5. Phosphate at milimolar concentrations inhibited the enzyme and this inhibitory effect was totally reversed as the concentrations of MgATP and MgADP rised to physiologically high levels. Na+ and K+ activated the enzyme in the absence of MgATP and MgADP. Both cations largely enhanced the Vmax with Na+ being more potent. A comparison of the kinetic behaviour of the enzyme in vitro with the metabolite concentrations in vivo suggest that a substantial regulation can occur through changes in AMP and Na+ concentrations.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"46-57"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12461046","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":"The effect of collagen degradation products (CDP) on the central nervous system (CNS).","authors":"E Telejko, J Maćkowiak, J Ksiazek, K Wiśniewski","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Rat collagen type I was digested with bacterial collagenase. The peptides obtained were submitted to gel filtration on Sephadex G-25. Two fractions differing in molecular weight (CDP I-3000 D and CDP II-1200 D) were obtained. These fractions administered to rats were found to have an inhibiting effect on the central nervous system (CNS) in Lat's test and the mobility of the animals recorded on a motimeter was found to be reduced. This effect was dependent on the peptide dose and occurred after intravenous (iv) as well as intraventricular (icv) injection.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"8-17"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12510682","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}
A Hołownia, M Chwiećko, D Pawłowska, R Farbiszewski
{"title":"The diminution of liver glutathione content and changes in activities of antioxidant enzymes in long-term acetaldehyde poisoning.","authors":"A Hołownia, M Chwiećko, D Pawłowska, R Farbiszewski","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effect of acetaldehyde administration for 4 weeks on antioxidant protection systems was investigated in liver of rats. Liver SOD activity was decreased from control value 542.4 U/g of tissue to 411.2 U/g of tissue in experimental group (24% decrease). GSH-Px activity was practically unchanged and liver CAT activity was significantly decreased (35%). Sulfhydryl compounds in liver non-proteins following ACH treatment were decreased from 4.22 mumol/g of tissue in control group to 2.86 mumol/g of tissue (23%). Furthermore acetaldehyde treatment caused significant increase in MDA level in liver (78% increase).</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"18-23"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12461042","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}
Z Skrzydlewski, R Rółkowski, K Worowski, C Lukaszuk
{"title":"Complexoproductive and antiheparin properties of low density lipoproteins (LDL). I. Interaction of isolated low density lipoproteins with heparin of different molecular weight.","authors":"Z Skrzydlewski, R Rółkowski, K Worowski, C Lukaszuk","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Low density lipoproteins/LDL/ form unsoluble complexes with heparin of different molecular weight in the presence of CaCl2. Quantity of the complexes depends on molecular weight of heparin, concentration of reagents and pH of the reacting medium. The biggest quantity of complexes result from LDL-heparin of the molecular weight 16000, the quantity is smaller with heparin of the molecular weight 5100 and the quantity is smallest with heparin of the molecular weight 3700. Components of LDL--heparin complexes are bound by means of ion and hydrogen bonds.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"24-31"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12510829","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":"Direct muscular neurotization as a method of treatment of irreparable nerve injuries.","authors":"J Monach, J Skowroński","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Authors have presented of 12 patients with irreparable nerve injuries treated by direct motor nerve implantation into muscle belly (direct muscular neurotization). Results were evaluated in Sunderland scale. Motor function of the neurotized muscles following 12 months from operation was in range of between M3 and M4.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"58-63"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12461047","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":"The serum immunoglobulins level in maxillofacial bacterial infections.","authors":"K Zółkowski, L Gruszewska-Lewczuk, K Zwierz","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The IgG, IgA and IgM levels in the serum of 23 patients with maxillofacial bacterial infections were determined. The high IgG level noted on admission further increased in the serum of 14 patients with acute inflammation and decreased in the serum of 10 patients with a chronic course. The level of IgM in the serum of patients with acute inflammation was higher than in the patients with chronic inflammation and decreased in both groups on the 7th day of treatment. The IgA level was high on admission in both groups and fell on the 7th day of treatment. Our results suggest that analysis of the serum level of IgG, IgA and IgM may be of diagnostic and prognostic value in the treatment of maxillofacial bacterial inflammation.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"64-70"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12461048","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":"The results of laminectomy and laminoplasty in cervical myeloradiculopathy.","authors":"J Skowroński, M Bielecki","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The authors present the results of laminectomy and laminoplasty in 20 patients with cervical myeloradiculopathy according to the JOA score. Improvement was noted in 74% of the patients after laminoplasty and in 70% of the patients after laminectomy. On the whole decompression is a good method of treatment in this kind of disease.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"71-3"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12461049","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":"The effect of quercetin and lithium ions on platelet aggregation.","authors":"M Tomasiak","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Quercetin inhibited aggregation of porcine blood platelets induced by collagen (IC50 = 0.2 mM), ADP (IC50 = 0.5 mM), thrombin (IC50 = 0.02 mM) and ionophore A23187 (IC50 = 1.5 mM). Preincubation of platelets with 10 mM LiCl abolished the inhibitory effect of quercetin on the aggregation of these cells induced by thrombin. Lithium ions per se caused potentiation of the aggregation of platelets induced by thrombin. Neither potentiation of aggregation by Li+, nor the abolishing of the inhibitory effect of quercetin by Li+ was observed when platelets were activated by ionophore A23187. Since lithium ions inhibit activity of enzymes degradating inositol phosphate, the obtained results can be interpreted to mean that quercetin affect platelet aggregation by the inhibition of inositol phosphates production.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"37 ","pages":"38-45"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12461045","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}