نتایج جستجو برای: hemoglobins

تعداد نتایج: 1615  

Journal: :Blood 1962
T G FERRIS R E EASTERLING R E BUDD

By THOMAS G. FERRIS, ROBERT E. EASTERLING AND RICHARD E. BUDD T HE VARIOUS types of hemoglobins have been identified and reported by means of zone electrophoresis using supporting media such as filter paper,’ starch,2 agar,3 cellulose acetate,4 and combinations of these media. Recently a synthetic acrylamide gel ( Cyanogum 41#{176} ) has been investigated and found to have characteristics which...

2001
JOHN A. JACQUEZ

Oxygen has a very low solubility in aqueous solutions, and with rare exceptions we find that oxygen is carried in the circulation almost entirely in combination with a special oxygen-binding protein. Four main types of such proteins are found in the animal kingdom: hemoglobins, chlorocruorins, hemerythrins, and hemocyanins. The most widely distributed in the animal kingdom are the hemoglobins, ...

Journal: :Blood 1967
H Kitchen F W Putnam W J Taylor

By H’ mit si KITCHEN, FRANK W . PUTNAM AND \V. JAPE TAYLOR I HE SICKLING OF ERYTHROCYTES under in vitro laboratory conditions has been demonstrated in most species of deer. This remarkable distortion of the erythrocytes from the biconcave disc shape to such bizarre forms as holly leaf, crescent and oat shapes in several species of deer was first described by Gulliver in 1840. Seventy years late...

Journal: :The Journal of biological chemistry 1972
L H Janssen S H de Bruin G A van Os

The titration curves of the human hemoglobins AZ and F, the slow and fast components of horse hemoglobin, and bovine hemoglobin B have been analyzed, mainly to obtain information about the titration behavior of the histidines in these hemoglobins. The results were also compared with earlier data concerning human hemoglobin A and bovine hemoglobin A. In both hemoglobin As and F, 18 titratable hi...

Journal: :The Journal of biological chemistry 2004
Takeshi Yokoyama Khoon Tee Chong Gentaro Miyazaki Hideki Morimoto Daniel T-B Shih Satoru Unzai Jeremy R H Tame Sam-Yong Park

The crystal structure of hemoglobin has been known for several decades, yet various features of the molecule remain unexplained or controversial. Several animal hemoglobins have properties that cannot be readily explained in terms of their amino acid sequence and known atomic models of hemoglobin. Among these, fish hemoglobins are well known for their widely varying interactions with heterotrop...

2001
Toshio Asakura

A spin label is attached covalently to a propionic acid group of the heme in either the a or B subunits of hemoglobin. Hemoglobins, so chemically modified, show functional properties similar to those of native hemoglobins. Since electron paramagnetic resonance is sensitive to the ligation state of hemoglobin, electron paramagnetic resonance changes have been used to “follow” the sequence of lig...

Journal: :Biochemistry 2006
Benoit J Smagghe Gautam Sarath Emily Ross Jean-Louis Hilbert Mark S Hargrove

Hexacoordinate hemoglobins are found in many living organisms ranging from prokaryotes to plants and animals. They are named "hexacoordinate" because of reversible coordination of the heme iron by a histidine side chain located in the heme pocket. This endogenous coordination competes with exogenous ligand binding and causes multiphasic relaxation time courses following rapid mixing or flash ph...

Journal: :medical laboratory journal 0
farshid fayyaz aja university of medical sciences, tehran, iran

abstract      background and objective: aluminum phosphide (alp) is a solid non-organic phosphide with dark gray or dark yellow crystals. it reacts with stomach acid after ingestion and causes phosphine gas to be released. it is thought that phosphine causes toxicity from enzymatic interference and may even lead to cell death. this study aimed to investigate the effects of poisoning with rice t...

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