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5.2.4 Bioactive Peptides from Hemoglobin Sources
In 1971, the first biologically active peptide was obtained from hemoglobin (Hb)
(Moeller et al. 1997). Hemoglobin is familiar as an origin of series of peptides
which can play miscellaneous biological roles. Hemoglobin is a tetramerous protein
with two α- and two β-globular chains. Each globular chain possesses a prosthetic
group i.e. heme portion and basically acts as oxygen carrier in oxidation-reduction
reactions and in tissues. In addition to tissues such as RBCs, α- and β-globular chain
encrypt in the brains and peripheral tissues of humans and rodents, many different
novel bioactive peptides were isolated from variants of hemoglobin which have
significant physiological functions (Gomes et al. 2010).
Neokyotorphin as a bioactive peptide is a globular chain of Hb with (137–141)
sequence at C terminal presenting originally the analgesic action like that of Leuenkephaline (Fukui et al. 1983; Kiso et al. 1983). Neokyotorphin peptide (137–141)
isolated from various sources i.e. bovine brain, heart of rat, lung and brain. Moreover,
it also exists in hibernating ground squirrel with variant biological actions. Except
for hemorphins, neokyotorphin has been imparted a series of role like regulation of
body temperature, modulation of antibacterial action, regulation of vagus nerve
action on heart, provide safety from convulsion in epileptic cases, regulation of
brain function of ground squirrel and multiplication in cancerous cells and in lipocytes (Hazato et al. 1986; Ueda et al. 1987; Kolaeva et al. 1990; Sazonova et al. 2003).
Kyotorphin, a non-opioid, BAP is also a globular chain fragment of Hb with
(140–141) sequence at C terminal is a potential analgesic agent mainly isolated
from different sources such as bovine brain, spinal cord of rat and brain of rat. Until
now, the target for its biological activity is still unknown (Takagi et al. 1979).
A BAP, Hemorphins, (Tyr-Pro-Trp-Thr) derived from β globin of hemoglobin at
N-terminal mainly reduces electrical contraction in GPI bioassay. Extended hemorphin peptides have been obtained from a variety of sources such as bovine and
human tissues. It has been found that hemorphin plays an antagonist role for receptors of opioids (Nyberg et al. 1997). Extended hemorphin-7 is considered as a powerful ligand for the IV receptor of angiotensin (Moeller et al. 1997; Moeller et al.
1999). LVV-hemorphin-7 was found to provide a protection to BAP from degradation process by inhibiting peptidases like insulin-regulated aminopeptidase (IRAP)
and minimize the Bp level by giving injection into the peritoneal cavity. Besides
these, in supersensitive rat, LVV-hemorphin 7 was noted to lower the heart rate
(Cejka et al. 2004). In insensible rats, it heightened the action that caused reduction
in Bp in bradykinin (Fruitier-Arnaudin et al. 2002). It is noteworthy that LVVhemorphin- 7 has significance in terms of reminiscence and acquisition of knowledge. As in rats, learning is boosted by administrating the injection of
LVV-hemorphin 7. It is thought that LVV-hemorphin-7 depicts undeviating action
on other focal points which causes the delivery of acetylcholine followed by depolarizing effect, heightening the cholinergic dionifus leading to upgraded reasoning
level (Herbst et al. 1997; Lee et al. 2001). Finally, the ability of LVV-hemorphin 7
is to provide safety to the surface of IRAP followed by blocking the action of IRAP
K. Mustafa et al.
5.2.4 Bioactive Peptides from Hemoglobin Sources
In 1971, the first biologically active peptide was obtained from hemoglobin (Hb)
(Moeller et al. 1997). Hemoglobin is familiar as an origin of series of peptides
which can play miscellaneous biological roles. Hemoglobin is a tetramerous protein
with two α- and two β-globular chains. Each globular chain possesses a prosthetic
group i.e. heme portion and basically acts as oxygen carrier in oxidation-reduction
reactions and in tissues. In addition to tissues such as RBCs, α- and β-globular chain
encrypt in the brains and peripheral tissues of humans and rodents, many different
novel bioactive peptides were isolated from variants of hemoglobin which have
significant physiological functions (Gomes et al. 2010).
Neokyotorphin as a bioactive peptide is a globular chain of Hb with (137–141)
sequence at C terminal presenting originally the analgesic action like that of Leuenkephaline (Fukui et al. 1983; Kiso et al. 1983). Neokyotorphin peptide (137–141)
isolated from various sources i.e. bovine brain, heart of rat, lung and brain. Moreover,
it also exists in hibernating ground squirrel with variant biological actions. Except
for hemorphins, neokyotorphin has been imparted a series of role like regulation of
body temperature, modulation of antibacterial action, regulation of vagus nerve
action on heart, provide safety from convulsion in epileptic cases, regulation of
brain function of ground squirrel and multiplication in cancerous cells and in lipocytes (Hazato et al. 1986; Ueda et al. 1987; Kolaeva et al. 1990; Sazonova et al. 2003).
Kyotorphin, a non-opioid, BAP is also a globular chain fragment of Hb with
(140–141) sequence at C terminal is a potential analgesic agent mainly isolated
from different sources such as bovine brain, spinal cord of rat and brain of rat. Until
now, the target for its biological activity is still unknown (Takagi et al. 1979).
A BAP, Hemorphins, (Tyr-Pro-Trp-Thr) derived from β globin of hemoglobin at
N-terminal mainly reduces electrical contraction in GPI bioassay. Extended hemorphin peptides have been obtained from a variety of sources such as bovine and
human tissues. It has been found that hemorphin plays an antagonist role for receptors of opioids (Nyberg et al. 1997). Extended hemorphin-7 is considered as a powerful ligand for the IV receptor of angiotensin (Moeller et al. 1997; Moeller et al.
1999). LVV-hemorphin-7 was found to provide a protection to BAP from degradation process by inhibiting peptidases like insulin-regulated aminopeptidase (IRAP)
and minimize the Bp level by giving injection into the peritoneal cavity. Besides
these, in supersensitive rat, LVV-hemorphin 7 was noted to lower the heart rate
(Cejka et al. 2004). In insensible rats, it heightened the action that caused reduction
in Bp in bradykinin (Fruitier-Arnaudin et al. 2002). It is noteworthy that LVVhemorphin- 7 has significance in terms of reminiscence and acquisition of knowledge. As in rats, learning is boosted by administrating the injection of
LVV-hemorphin 7. It is thought that LVV-hemorphin-7 depicts undeviating action
on other focal points which causes the delivery of acetylcholine followed by depolarizing effect, heightening the cholinergic dionifus leading to upgraded reasoning
level (Herbst et al. 1997; Lee et al. 2001). Finally, the ability of LVV-hemorphin 7
is to provide safety to the surface of IRAP followed by blocking the action of IRAP
K. Mustafa et al.