Sentences with phrase «of myoglobin»

Finally, in 2013, Michael Berenbrink of Liverpool Univ. and Kevin Campbell of the Univ. of Manitoba noted that deep - diving mammals expressed large amounts of myoglobin in their muscle tissue.

Samuel said the stability differences aren't obvious if one simply compares the overall structures of the myoglobin from each species.

In a tenth grade honors biology course in 1978 he learned about the structure of myoglobin, which had been recently solved.

[6] Type IIB fibres contain a low content of myoglobin, relatively few mitochondria, relatively few blood capillaries and large amounts glycogen.

Myoglobin is the molecule that transports oxygen around the body; it is red in color, therefore the muscles which are used a lot contain a lot of myoglobin and will be deep red.

The color was a problem: Because of a lack of myoglobin — an oxygen - binding protein in muscle fibers — the cultured meat looked white instead of red.

Samuel, a graduate student in the Department of BioSciences at Rice, said the heme - free form of myoglobin that she studied is called apoprotein or apomyoglobin.

In her tests, Samuel compared the stability and cell - free expression level of myoglobins from humans, pigs, goosebeak whales, gray seals, sperm whales, dwarf sperm whales and the three mutants, which had low heme affinity but were 50 times more stable than apomyoglobins from the whales.

Myoglobin holds oxygen for ready use inside muscle cells, and the study found that marine mammals have ultra-stable versions of myoglobin that tend not to unfold.

Outcomes include permanent loss of brain function, acute tubular necrosis in the kidneys, and even, for people active in a heat wave, the leakage of myoglobin from broken skeletal muscle cells, resulting in toxins in the liver and lungs.

The researchers found that stability was the key for cells to make large amounts of myoglobin, which is explains why deep - diving mammals can load their muscle cells with far more myoglobin than humans.

[3] Type IIx fibres contain a low content of myoglobin, relatively few mitochondria, relatively few blood capillaries and large amounts glyrs are red

We found that the stability of heme - free myoglobin is the key factor that allows cells to produce high amounts of myoglobin.»

[6] They contain very large amounts of myoglobin, very many mitochondria and very many blood capillaries.

Tripe is also a «white» meat (meaning it has a low amount of myoglobin, the protein that makes red meat red), and has historically been used for dogs with sensitive digestive tracts, or food allergies.