Protein as Palat
trasnportasi / carrier.
Transporter protein has the ability to bind to
specific molecules and transporting various substances through the blood
stream. For instance:
hemoglobin,
consisting of group-containing compound heme iron bound to the protein globin,
serves as an oxygen carrier in the blood of vertebrates;
myoglobin, the oxygen transporter in muscle
tissue;
Serum albumin, as a
transporter of fatty acids in the blood;
ceruloplasmin, a
copper ion transporters in darah.
-EXPLANATION
--Hemoglobin
(short: Hb) is protein
molecule in red blood cells that combine with oxygen and carbon dioxide to be
transported through the circulatory system to the tissue-tissue in the body.
iron ions in the form of Fe 2 in hemoglobin gives red color to the blood.
Normally 100 ml of blood contains 15 grams of hemoglobin capable of carrying
human hemoglobin 0:03 oksigen.
Molecul gram terbina
than four subunit protein globule form (namely near-Sfera). Therefore one
subunit can carry one molecule of oxygen, it is effective every molecule of
hemoglobin can carry four oxygen molecules. Each subunit also composed than one
polypeptide chain that binds strongly the other molecules, called heme heme.
sturucture is more or
less the same as chlorophyll. It consists instead of a ring-shaped protein
molecule is not called porphyrin, and one atom of iron (Fe), located in the
middle of last porphyrin molecule. This is where oxygen will be bound during
the blood through the lungs
.
--Cerum albumin
is a protein called albuminSering with the
highest number in the body. Albumin is essential for maintaining the osmotic
pressure on the distribution of body fluids between intravascular compartment
and tubuh.Albumin network also serves as a carrier plasma by indirectly binding
hydrophobic steroid hormones and protein bearers for hemin and fatty acids in
sirkulasinya.
BSA, fraction V of
serum albumin is useful to shed some substance from the blood circulation
through the liver, such as bilirubin, thyroxine, taurolithocholic acid, chenodeoxycholic
acid, and heme digitoksin peptides of cytochrome C. [5] 60% of the proteins in
blood plasma, serum amount that exceeds normal limits can be harmful to humans.
Prealbumin (English: transthyretin) is suspected as the bearers of hormone thyroxine
from the blood to the brain.
--Seruloplasmin
copper compete for
absorption in the digestive tract, causing one of the advantages of these
minerals in the diet lead to mineral deficiencies feeds the other. RDA copper
for a healthy adult is 0.9 mg daily. Copper is transported most of the
bloodstream by plasma protein called ceruloplasmin. When copper was first
absorbed in the stomach, he was transported to hatidan bound albumin.
cooper have an important role in a number of plant and animal enzymes, including
cytochrome c oxidase copper-centered and enzymes superoxide dismutase (contains
copper and zinc). Particularly those involved in catalysis and electron
transfer in dioxygen transport and catalysis reaction.
Blue copper protein involved in the transport
of electrons and plastosianin termasuklah azurin.
Blue copper name derived than
blue terhasil strong absorption lines due to the transport of ligand to metal
charge around 600 nm. In the oxygenation reaction of tyrosinase, ascorbate
oxidase, and for the transport of oxygen (hemocyanin). Most of the biologically
active copper centers found in proteins outside the cell or vesicle.
--Myoglobin
is a monomeric protein tertiary function is to
keep a back up oxygen in skeletal muscle cells (striated muscle). Protein is
made up of approximately 154 amino acid sequence and contains a single heme
group (porphyrin chains containing one iron atom). Gena which encodes the
protein myoglobin consists of three ekson.Protein myoglobin is composed of
eight alpha chain named after the latin alphabet (A through H)
unlike hemoglobin
which has four heme groups, myoglobin has only one functioning piece heme group
binds intracellular oxygen. Cluster heme is bound by a histidine side chain, ie
the chain near the histidine (proximal) that bind heme directly in the chain of
hydrophobic proteins and histidine far (distal), which serves to stabilize the
heme is bound oxygen
.
Cluster histidine
far also provide protection from the molecules of carbon monoxide (CO) which
can enter into myoglobin.Oksigen will be used for the formation of ATP, which
takes place in the mitochondrial matrix. Without the help of oxygen, the
process of formation of ATP in the mitochondria will be uninterrupted.