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Identification of Intracellular Carbonic Anhydrase in Chlamydomonas reinhardtii with a Carbonic Anhydrase-Directed Photoaffinity Label

Autor: H. D. Husic, C. A. Marcus

Publikováno v: Plant Physiology. 105:133-139

A carbonic anhydrase (CA)-directed photoaffinity reagent, 125I-labeled p-aminomethylbenzenesulfonamide-4-azidosalicylamide,was synthesized and shown to derivatize periplasmic CA in the unicellular green alga Chlamydomonas reinhardtii. The photoderiva

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2917cf56b1f61b047984f72c499cffdb
https://doi.org/10.1104/pp.105.1.133

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Intracellular carbonic anhydrase of Chlamydomonas reinhardtii

Autor: Jan Karlsson, Zm Ramazanov, H. D. Husic, Göran Samuelsson, Thomas Hiltonen

Publikováno v: Plant physiology. 109(2)

An intracellular carbonic anhydrase (CA; EC 4.2.1.1) was purified to homogeneity from a mutant strain of Chlamydomonas reinhardtii (CW 92) lacking a cell wall. Intact cells were washed to remove periplasmic CA and were lysed and fractionated into sol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5786e249a23bb91df946ddc613c2abce
https://pubmed.ncbi.nlm.nih.gov/7480345

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Salt-Induced Dissociation of Carbonic Anhydrase from Intact Cells of Chlamydomonas reinhardtii

Autor: H. D. Husic, E A Quigley

Publikováno v: Plant physiology. 94(1)

The extracellular carbonic anhydrase of Chlamydomonas reinhardtii is dissociated from either intact or lysed cells by treatment with a 20 millimolar potassium phosphate buffer containing 0.4 molar KCI at pH 7.4. Electrophoretic analysis of proteins d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63e20c5d24e6b917f8c3845a1b823fb2
https://pubmed.ncbi.nlm.nih.gov/16667713

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Muscle cell cultures from chicken breast muscle have increased specific activities of creatine kinase when incubated at 41 °C compared with 37 °C

Autor: Clarence H. Suelter, Elizabeth A. Cowles, V D Bennett, H D Husic

Publikováno v: Experimental Cell Research. 164:63-70

Chicken muscle cell cultures were incubated at 41 degrees C, the physiological chicken body temperature, and compared with cultures incubated at 37 degrees C, the typical cell culture incubation temperature. The cultures incubated at 41 degrees C sho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ffa68b4d93614722363fc8d3da23da0f
https://doi.org/10.1016/0014-4827(86)90454-4

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The levels of creatine kinase and adenylate kinase in the plasma of dystrophic chickens reflect the rates of loss of these enzymes from the circulation

Autor: H D Husic, Clarence H. Suelter

Publikováno v: Biochemical Medicine. 29:318-336

The rates of loss of adenylate kinase and creatine kinase from the circulation after intravenous injection of homogenous chicken skeletal muscle enzymes were examined to determine the role of plasma clearance rates in determining the plasma levels of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c16ab659c91062c17c9308bfa54d8883
https://doi.org/10.1016/0006-2944(83)90068-6

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Circulatory clearance, internalization, and degradation of muscle AMP aminohydrolase

Autor: C H Suelter, H D Husic

Publikováno v: Journal of Biological Chemistry. 259:4359-4364

Chicken muscle AMP aminohydrolase is cleared rapidly from the circulation of chickens after intravenous injection of the purified enzyme (Husic, H. D., and Suelter, C. H. (1980) Biochem. Biophys. Res. Commun. 95, 228-235). After the intravenous injec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c5de04ee13cf398047b3f30e85c3c5bb
https://doi.org/10.1016/s0021-9258(17)43054-7

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Binding, internalization, and degradation of AMP aminohydrolase by avian hepatocyte monolayers

Autor: C H Suelter, H D Husic

Publikováno v: Journal of Biological Chemistry. 259:4365-4371

Chicken muscle AMP aminohydrolase is cleared from the circulation of chickens after intravenous injection of the purified enzyme with a half-life of 3-5 min (Husic, H.D., and Suelter, C.H. (1980) Biochem. Biophys. Res. Commun. 95, 228-235). The enzym

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bda76703897f285e3afb960b7170d452
https://doi.org/10.1016/s0021-9258(17)43055-9

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Circulatory clearance, internalization, and degradation of muscle AMP aminohydrolase

Autor: H D, Husic, C H, Suelter

Publikováno v: The Journal of biological chemistry. 259(7)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::aa1022578b298ad307c28eb297aa08a3
https://pubmed.ncbi.nlm.nih.gov/6707009

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Muscle cell cultures from chicken breast muscle have increased specific activities of creatine kinase when incubated at 41 degrees C compared with 37 degrees C

Autor: V D, Bennett, E, Cowles, H D, Husic, C H, Suelter

Publikováno v: Experimental cell research. 164(1)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::658835a2e215375fe71ca166dbd0dfa5
https://pubmed.ncbi.nlm.nih.gov/3956598

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Binding, internalization, and degradation of AMP aminohydrolase by avian hepatocyte monolayers

Autor: H D, Husic, C H, Suelter

Publikováno v: The Journal of biological chemistry. 259(7)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f68d7bc6d4a2effe066dd62b418c20da
https://pubmed.ncbi.nlm.nih.gov/6707010

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