The School of Biomedical Sciences Wiki - User contributions [en]

Cardiac Arrythmia

2012-10-21T12:05:49Z

110029432:

Irregularity in the rhythm of the heart beat as well as an abnormal heart rate is known as Cardiac Arrythmia. There is a wide variety of causes of arrythmia, such as injury caused by heart attacks and coronary heart disease.  Arrythmia can be diagnosed by its symptoms which include pounding of the chest, fatigue, palpitations as well as shortness of breath and fainting.  <ref>http://www.medicinenet.com/arrhythmia_irregular_heartbeat/article.htm</ref><references />

Cardiac Arrythmia

2012-10-21T12:03:50Z

110029432: Created page with "Irregularity in the rhythm of the heart beat as well as an abnormal heart rate is known as Cardiac Arrythmia. There is a wide variety of causes of arrythmia, such as injury cause..."

Irregularity in the rhythm of the heart beat as well as an abnormal heart rate is known as Cardiac Arrythmia. There is a wide variety of causes of arrythmia, such as injury caused by heart attacks and coronary heart disease. 

Arrythmia can be diagnosed by its symptoms which include pounding of the chest, fatigue, palpitations as well as shortness of breath and fainting. 

 

<ref>http://www.medicinenet.com/arrhythmia_irregular_heartbeat/page2.htm</ref>

Structure of Haemoglobin

2011-11-30T15:14:10Z

110029432:

Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to Haemoglobin is related to its structure, and the rate of efficacy is further related to this. Haemoglobin found in mammals is composed of 4 subunits, and, thus, is known as tetrameric: they are further divided into 2 types: 2 are α, and 2 are β subunits <ref>Voet D., Voet J G., Pratt C W., (1999) Fundamentals of Biochemistry, New York: Wiley. Page 165</ref>. The quaternary structure of Haemoglobin changes upon it's binding of oxygen to maximise efficiency in areas of high pO2, and likewise the shape of Haemoglobin changes when off-loading Haemoglobin at areas of low pO2: this permits the delivery of the maximum amount of oxygen. Changes in shape include the rotation of the α1β1 and α2β2 dimers upon binding with oxygen; this change allows them to move with greater ease in order to deliver oxygen around the body <ref>Berg J., Tymoczko J. and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman. Page 210</ref>

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Structure of Haemoglobin

2011-11-30T15:13:22Z

110029432:

Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to Haemoglobin is related to its structure, and the rate of efficacy is further related to this. Haemoglobin found in mammals is composed of 4 subunits, and, thus is known as tetrameric: they are further divided into 2 types: 2 are α, and 2 are β subunits <ref>Voet D., Voet J G., Pratt C W., (1999) Fundamentals of Biochemistry, New York: Wiley. Page 165</ref>. The quaternary structure of Haemoglobin changes upon it's binding of oxygen to maximise efficiency in areas of high pO2, and likewise the shape of Haemoglobin changes when off-loading Haemoglobin at areas of low pO2: this permits the delivery of the maximum amount of oxygen. Changes in shape include the rotation of the α1β1 and α2β2 dimers upon binding with oxygen; this change allows them to move with greater ease in order to deliver oxygen around the body <ref>Berg J., Tymoczko J. and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman. Page 210</ref>

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Structure of Haemoglobin

2011-11-30T15:12:31Z

110029432:

Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to Haemoglobin is related to its structure, and the rate of efficacy is further related to this. Haemoglobin found in mammals is composed of 4 subunits, and, thus is known as tetrameric: they are further divided into 2 types: 2 are α, and 2 are β subunits <ref>Voet D., Voet J G., Pratt C W., (1999) Fundamentals of Biochemistry, New York: Wiley. Page 165</ref>. The quaternary structure of Haemoglobin changes upon it's binding of oxygen to maximise efficiency in areas of high pO2, and likewise the shape of Haemoglobin changes when off-loading Haemoglobin at areas of low pO2: this permits the delivery of the maximum amount of oxygen. Changes in shape include the rotation of the α1β1 and α2β2 dimers upon binding with oxygen; this change allows them to move with greater ease in order to deliver oxygen around the body

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<ref>Berg J., Tymoczko J. and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman. Page 210</ref><references />.

Structure of Haemoglobin

2011-11-30T15:11:30Z

110029432:

Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to Haemoglobin is related to its structure, and the rate of efficacy is further related to this. Haemoglobin found in mammals is composed of 4 subunits, and, thus is known as tetrameric: they are further divided into 2 types: 2 are α, and 2 are β subunits <ref>Voet D., Voet J G., Pratt C W., (1999) Fundamentals of Biochemistry, New York: Wiley. Page 165</ref><references />. The quaternary structure of Haemoglobin changes upon it's binding of oxygen to maximise efficiency in areas of high pO2, and likewise the shape of Haemoglobin changes when off-loading Haemoglobin at areas of low pO2: this permits the delivery of the maximum amount of oxygen. Changes in shape include the rotation of the α1β1 and α2β2 dimers upon binding with oxygen; this change allows them to move with greater ease in order to deliver oxygen around the body <ref>Berg J., Tymoczko J. and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman. Page 210</ref><references />.

Structure of Haemoglobin

2011-11-30T15:11:00Z

110029432:

Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to Haemoglobin is related to its structure, and the rate of efficacy is further related to this. Haemoglobin found in mammals is composed of 4 subunits, and, thus is known as tetrameric: they are further divided into 2 types: 2 are α, and 2 are β subunits <ref>Voet D., Voet J G., Pratt C W., (1999) Fundamentals of Biochemistry, New York: Wiley. Page 165</ref>. The quaternary structure of Haemoglobin changes upon it's binding of oxygen to maximise efficiency in areas of high pO2, and likewise the shape of Haemoglobin changes when off-loading Haemoglobin at areas of low pO2: this permits the delivery of the maximum amount of oxygen. Changes in shape include the rotation of the α1β1 and α2β2 dimers upon binding with oxygen; this change allows them to move with greater ease in order to deliver oxygen around the body <ref>Berg J., Tymoczko J. and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman. Page 210</ref>.

Structure of Haemoglobin

2011-11-30T15:07:30Z

110029432: Created page with "Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to Haemoglobin is related to its ..."

Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to Haemoglobin is related to its structure, and the rate of efficacy is further related to this. Haemoglobin found in mammals is composed of 4 subunits, and, thus is known as tetrameric: they are further divided into 2 types: 2 are α, and 2 are β subunits <references /> . The quaternary structure of Haemoglobin changes upon it's binding of oxygen to maximise efficiency in areas of high pO2, and likewise the shape of Haemoglobin changes when off-loading Haemoglobin at areas of low pO2: this permits the delivery of the maximum amount of oxygen. Changes in shape include the rotation of the α1β1 and α2β2 dimers upon binding with oxygen; this change allows them to move with greater ease in order to deliver oxygen around the body <references />.