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The International journal of biochemistry最新文献

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Clearance of certain modified haptoglobins from the rabbit circulation. 清除兔循环中某些修饰的触珠蛋白。
The International journal of biochemistry Pub Date : 1988-01-01 DOI: 10.1016/0020-711x(88)90359-x
W Dobryszycka, T Guszczyński, Z Kubicz
{"title":"Clearance of certain modified haptoglobins from the rabbit circulation.","authors":"W Dobryszycka,&nbsp;T Guszczyński,&nbsp;Z Kubicz","doi":"10.1016/0020-711x(88)90359-x","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90359-x","url":null,"abstract":"<p><p>1. Human haptoglobin (Hp) type 2-1 was subjected to the sulfanilazo-modification of tyrosine and histidine residues, the removal of sialic acid, and the reduction of disulfide bonds (isolation of alpha 2, alpha 1, beta subunits), respectively. Radioactively labeled preparations were administered intravenously to rabbits. 2. Human Hp and isolated beta (heavy) chain disappeared from the circulation somewhat faster (half-lives = 72 and 67 h, respectively), than homologous rabbit Hp (half-life = 96 h). Hp light chains (alpha 2, alpha 1), devoid of oligosaccharide showed shorter half-lives of 27-19 h. 3. Treatment of Hp with diazotized sulfanilic acid resulted in an appreciable reduction of half-life to 21-11 h, as dependent on the number of modified residues. 4. Asialo-Hp, asialo-beta chain, and asialo-sulfanilazo-Hp were cleared rapidly from the circulation with half-lives of 5.5, 5.0, and 4.2 h, respectively. 5. These results suggest that in different pathways of Hp catabolism in vivo, polypeptide recognition markers in addition to carbohydrate ones, are involved.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"20 3","pages":"325-8"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90359-x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14481975","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}
引用次数: 3
Cysteine proteinase inhibitors from rabbit skeletal muscle. 兔骨骼肌半胱氨酸蛋白酶抑制剂。
The International journal of biochemistry Pub Date : 1988-01-01 DOI: 10.1016/0020-711x(88)90349-7
M Matsuishi, A Okitani, Y Hayakawa, H Kato
{"title":"Cysteine proteinase inhibitors from rabbit skeletal muscle.","authors":"M Matsuishi,&nbsp;A Okitani,&nbsp;Y Hayakawa,&nbsp;H Kato","doi":"10.1016/0020-711x(88)90349-7","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90349-7","url":null,"abstract":"<p><p>1. Two cysteine proteinase inhibitors, I-T (Mr = 29,000) and I-S (Mr = 10,700), were isolated from rabbit skeletal muscle by means of succesive extraction with a neutral buffer solution, precipitation at pH 3.7, acetone fractionation and gel permeation on Sephadex G-75. 2. I-T is a formed trimer of a monomeric inhibitor, I-M (Mr = 10,500), through disulfide bonds. 3. I-S is almost completely stable between pH 3 and 8, while I-M is unstable in the same pH range. 4. I-M acts most effectively towards cathepsins H and L, showing moderate activity towards cathepsin B and only weak activity towards papain. I-S acts most effectively towards cathepsin L, followed by, in decreasing order, cathepsin H, cathepsin B and papain.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"20 3","pages":"259-64"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90349-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14482760","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}
引用次数: 13
Regulation of the first step of the histidine biosynthesis in Escherichia coli. 大肠杆菌组氨酸生物合成第一步的调控。
The International journal of biochemistry Pub Date : 1988-01-01 DOI: 10.1016/0020-711x(88)90346-1
T Dall-Larsen
{"title":"Regulation of the first step of the histidine biosynthesis in Escherichia coli.","authors":"T Dall-Larsen","doi":"10.1016/0020-711x(88)90346-1","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90346-1","url":null,"abstract":"","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"20 3","pages":"231-5"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90346-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14410201","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}
引用次数: 4
Effect of age and day time on the adenosine modulation of basal and insulin-stimulated glucose transport in rat adipocytes. 年龄和白天时间对腺苷调节基础和胰岛素刺激的大鼠脂肪细胞葡萄糖转运的影响。
The International journal of biochemistry Pub Date : 1988-01-01 DOI: 10.1016/0020-711x(88)90351-5
P Bush, J E Souness, V Chagoya de Sánchez
{"title":"Effect of age and day time on the adenosine modulation of basal and insulin-stimulated glucose transport in rat adipocytes.","authors":"P Bush,&nbsp;J E Souness,&nbsp;V Chagoya de Sánchez","doi":"10.1016/0020-711x(88)90351-5","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90351-5","url":null,"abstract":"<p><p>1. The relationship between the activity of adenosine metabolizing enzymes 5'nucleotidase (5'N), adenosine kinase (A.K.) and adenosine deaminase (A.D.) with basal and insulin-stimulated glucose transport in isolated fat cells from young and old animals was studied at 08:00 and 16:00 hr. 2. In cells from young animals a larger insulin-stimulation of glucose transport was observed at 16:00 hr than at 08:00 hr. Also at 16:00 hr small changes in 5'N, A.K. and A.D. activities suggest a decrease in adenosine formation. 3. In the cells from old animals no effect of insulin was observed at any time, while a 3-5-fold increase in 5'N indicated a predominance of adenosine formation at both times studied. 4. An inverse relationship was observed in the changes of adenosine metabolism and insulin action.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"20 3","pages":"279-83"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90351-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14409306","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}
引用次数: 5
In vitro activation of the contact activation system (Hageman factor system) in plasma by acidic phospholipids and the inhibitory effect of beta 2-glycoprotein I on this activation. 酸性磷脂体外激活血浆接触激活系统(Hageman因子系统)及β 2-糖蛋白I对该激活的抑制作用。
The International journal of biochemistry Pub Date : 1988-01-01 DOI: 10.1016/0020-711x(88)90356-4
I Schousboe
{"title":"In vitro activation of the contact activation system (Hageman factor system) in plasma by acidic phospholipids and the inhibitory effect of beta 2-glycoprotein I on this activation.","authors":"I Schousboe","doi":"10.1016/0020-711x(88)90356-4","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90356-4","url":null,"abstract":"<p><p>1. Negatively charged phospholipids promote initiation of the contact activation system in the blood coagulation. 2. Neutral phospholipids were unable to activate this system. 3. The activation is inhibited by beta 2-glycoprotein I at physiological concentrations. 4. The results raise the question whether people with low concentration of beta 2-glycoprotein I are more easily exposed to blood coagulation defects, such as disseminated intravascular coagulation, than those with normal concentration of beta 2-glycoprotein I.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"20 3","pages":"309-15"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90356-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14481972","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}
引用次数: 27
Fructose 2,6-bisphosphate-dependent regulation of phosphofructokinase in rat submandibular gland. 果糖2,6-二磷酸对大鼠颌下腺磷酸果糖激酶的依赖性调节。
The International journal of biochemistry Pub Date : 1988-01-01 DOI: 10.1016/0020-711x(88)90347-3
H Sugiya, Y Fujita, E Fukushima, T Yamazaki, S Furuyama
{"title":"Fructose 2,6-bisphosphate-dependent regulation of phosphofructokinase in rat submandibular gland.","authors":"H Sugiya,&nbsp;Y Fujita,&nbsp;E Fukushima,&nbsp;T Yamazaki,&nbsp;S Furuyama","doi":"10.1016/0020-711x(88)90347-3","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90347-3","url":null,"abstract":"<p><p>1. Regulation of phosphofructokinase in rat submandibular gland was non-Michaelis-Menten type at physiological pH. 2. At pH 7.3, ATP played a dual role on phosphofructokinase acting as a substrate and inhibitor at high concentration of ATP. 3. The activator of phosphofructokinase was present in cytosol fraction, and its properties were resemble to those of fructose 2,6-bisphosphate. 4. Both the activator and authentic fructose 2,6-bisphosphate relieved the inhibition of phosphofructokinase by ATP, and increased the affinity for fructose 6-phosphate. 5. Concentration of fructose 2,6-bisphosphate in rat submandibular gland was 8.22 nmol/g tissue, and which was about the half of that in liver. 6. Phosphofructokinase in rat submandibular gland was found to be regulated synergistically by ATP, fructose 6-phosphate and fructose 2,6-bisphosphate.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"20 3","pages":"237-41"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90347-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14099822","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}
引用次数: 7
Characterization of ATPase activity in the mycelial form cells of yeast Saccharomycopsis fibuligera. 酵母菌丝状细胞中atp酶活性的研究。
The International journal of biochemistry Pub Date : 1988-01-01
A Ota, H Morishita
{"title":"Characterization of ATPase activity in the mycelial form cells of yeast Saccharomycopsis fibuligera.","authors":"A Ota,&nbsp;H Morishita","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>1. The properties of ATPase activity were studied with the mycelial form cells of Saccharomycopsis fibuligera. 2. Optimal pH for the activity was about 9.5. 3. The activity was stimulated by Mg2+. 4. The activity was inhibited by DCCD, NaF and oligomycin, but not inhibited by ouabain.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"20 2","pages":"147-54"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14099742","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}
引用次数: 0
Development of brain insulin receptors. 脑胰岛素受体的发育。
The International journal of biochemistry Pub Date : 1988-01-01 DOI: 10.1016/0020-711x(88)90345-x
D LeRoith, W L Lowe, J Shemer, M K Raizada, A Ota
{"title":"Development of brain insulin receptors.","authors":"D LeRoith,&nbsp;W L Lowe,&nbsp;J Shemer,&nbsp;M K Raizada,&nbsp;A Ota","doi":"10.1016/0020-711x(88)90345-x","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90345-x","url":null,"abstract":"","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"20 3","pages":"225-30"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90345-x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14410200","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}
引用次数: 23
Effect of temperature on the kinetics of the yeast AMP deaminase. 温度对酵母菌AMP脱氨酶动力学的影响。
The International journal of biochemistry Pub Date : 1986-01-01
M Yoshino, K Murakami
{"title":"Effect of temperature on the kinetics of the yeast AMP deaminase.","authors":"M Yoshino,&nbsp;K Murakami","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The temperature dependence of the kinetics of the yeast AMP deaminase was examined using the purified enzyme and the permeabilized yeast cells. The increase in the enzyme affinity for the substrate AMP was accompanied by the decrease in the maximal velocity with the decreasing temperature in the absence and presence of ATP. The apparent Km for AMP was lowest at 15-20 degrees C, and the affinity was decreased below and above this temperature. The rate of the AMP deaminase reaction remained constant over a wide range of temperature in the presence of physiological AMP concentrations. The temperature dependent change in kinetic properties of AMP deaminase may contribute to the control of the yeast glycolytic flux under the condition of lower temperature environments.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"18 3","pages":"235-9"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14638514","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}
引用次数: 0
Kinetics of the interactions of the chicken erythrocyte AMP deaminase with anthraquinone compounds. 鸡红细胞AMP脱氨酶与蒽醌类化合物相互作用动力学研究。
The International journal of biochemistry Pub Date : 1986-01-01
M Yoshino, Y Kawamura
{"title":"Kinetics of the interactions of the chicken erythrocyte AMP deaminase with anthraquinone compounds.","authors":"M Yoshino,&nbsp;Y Kawamura","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Alizarine sulfonate, the anthraquinone containing both sulfonate and hydroxyl groups, showed an activating and inhibitory effect on the chicken erythrocyte AMP deaminase (EC 3.5.4.6). The cooperative effect of AMP, analyzed in terms of Hill coefficient, was decreased from 2.4 to 1.1 with the increase in the dye concentration, suggesting the dye as an allosteric activator of the enzyme. However, alizarine sulfonate acted as a mixed type inhibitor in the presence of higher level of AMP. The action of alizarine sulfonate can be accounted for by assuming that the dye binds to the enzyme at the allosteric-activating sites with a broad specificity toward nucleotide binding, and further at the specific inhibitory sites.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"18 3","pages":"241-4"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15069732","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}
引用次数: 0
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