Final Answer:
The red pigment in striated muscle which aids oxygen storage is myoglobin.
Step-by-step explanation:
Myoglobin is a crucial protein found in striated (skeletal and cardiac) muscle tissues that plays a significant role in oxygen storage. It contains a heme group, which is a complex of iron and porphyrin, giving myoglobin its characteristic reddish color. The iron within the heme group binds to oxygen, allowing myoglobin to store and release oxygen as needed by muscle cells during periods of increased activity or when oxygen supply is limited.
In the muscle tissue, myoglobin functions as an oxygen reservoir, facilitating the diffusion of oxygen from the bloodstream to the muscle cells. This is particularly important in situations where rapid oxygen delivery is required, such as during strenuous physical activity. The ability of myoglobin to bind and release oxygen is influenced by factors like oxygen tension, pH, and temperature, ensuring efficient oxygen transport based on the dynamic needs of the muscle.
The red coloration of myoglobin is the result of its iron-containing heme group, which is similar to the heme found in hemoglobin, the oxygen-carrying molecule in red blood cells. However, while hemoglobin primarily transports oxygen through the bloodstream, myoglobin is specifically designed to enhance oxygen storage within muscle cells, contributing to the overall oxygen supply and utilization in striated muscle tissues.