نتایج جستجو برای: myoglobin

تعداد نتایج: 4027  

Journal: :The Journal of experimental biology 2010
U B Hendgen-Cotta U Flögel M Kelm T Rassaf

For more than 100 years, myoglobin has been among the most extensively studied proteins. Since the first comprehensive review on myoglobin function as a dioxygen store by Millikan in 1939 and the discovery of its structure 50 years ago, multiple studies have extended our understanding of its occurrence, properties and functions. Beyond the two major roles, the storage and the facilitation of di...

Journal: :The Journal of experimental biology 2010
Gerolf Gros Beatrice A Wittenberg Thomas Jue

Myoglobin, a mobile carrier of oxygen, is without a doubt an important player central to the physiological function of heart and skeletal muscle. Recently, researchers have surmounted technical challenges to measure Mb diffusion in the living cell. Their observations have stimulated a discussion about the relative contribution made by Mb-facilitated diffusion to the total oxygen flux. The calcu...

Journal: :The Journal of experimental biology 2010
Michael Berenbrink

Myoglobin is a small, 17kDa, monomeric, O 2-binding haemoprotein that typically occurs in cardiac and aerobic skeletal muscle of vertebrates. Its classic function is the short-and long-term buffering of muscle O 2 concentrations during bursts of exercise or breath-hold diving and the facilitated diffusion of O 2 from blood to mitochondria (Wittenberg and Wittenberg, 2003). Determination of the...

Journal: :Biochemical Journal 1966

1999
ANDREW E. ARAI CLAUDIA E. KASSERRA PAUL R. TERRITO AMIR H. GANDJBAKHCHE ROBERT S. BALABAN

Arai, Andrew E., Claudia E. Kasserra, Paul R. Territo, Amir H. Gandjbakhche, and Robert S. Balaban. Myocardial oxygenation in vivo: optical spectroscopy of cytoplasmic myoglobin and mitochondrial cytochromes. Am. J. Physiol. 277 (Heart Circ. Physiol. 46): H683–H697, 1999.— The oxygenation state of myoglobin and the redox state of cytochrome c provide information on the PO2 in the cytosol and mi...

Journal: :The Journal of Experimental Medicine 1988
S J Brett K B Cease J A Berzofsky

Two lines of evidence in the current study indicate that antigen processing is a major factor, in addition to MHC binding and T cell repertoire, that determines Ir gene responsiveness and epitope immunodominance. First, immunization with synthetic peptides of myoglobin sequences revealed new reactivities that had not appeared after priming with native myoglobin. For example, B10.S mice (H-2S) i...

Journal: :PloS one 2016
Rachel Cartwright Cori Newton Kristi M West Jim Rice Misty Niemeyer Kathryn Burek Andrew Wilson Alison N Wall Jean Remonida-Bennett Areli Tejeda Sarah Messi Lila Marcial-Hernandez

For marine mammals, the ability to tolerate apnea and make extended dives is a defining adaptive trait, facilitating the exploitation of marine food resources. Elevated levels of myoglobin within the muscles are a consistent hallmark of this trait, allowing oxygen collected at the surface to be stored in the muscles and subsequently used to support extended dives. In mysticetes, the largest of ...

Journal: :Comparative biochemistry and physiology. Part A, Molecular & integrative physiology 2000
S R Noren T M Williams

Cetaceans exhibit an exceptionally wide range of body mass that influence both the capacities for oxygen storage and utilization; the balance of these factors is important for defining dive limits. Furthermore, myoglobin content is a key oxygen store in the muscle as it is many times higher in marine mammals than terrestrial mammals. Yet little consideration has been given to the effects of myo...

2007

Changes in pigments and color of sardine and mackerel muscles during iced storage were investigated. When the storage time increased, a gradual increase in pH was observed. The total extractable pigment and heme iron content decreased (P<0.05), while the non-heme iron content tended to increase throughout storage. The soret band of myoglobin decreased with the concomitant decrease in redness in...

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