ABSTRACTBackground : Acne vulgaris is a
common skin disease, affecting more than 85% of
adolescents and often continuing into adulthood.
People between 11 and 30 years of age and up to
5% of older adults. For most patients acne remains
a nuisance with occasional flares of unsightly
comedones, pustules and nodules. For other less
fortunate persons, the sever inflammatory response
to Propionibacterium acnes (P.acnes) results in
permanent
Methods: Disfiguring scars. (1, 2) Stigmata of sever
acne cane lead to social ostracism, withdrawal
from society and severe psychologic
depression (1-4).
Result Pathogenesis of acne Traditionally, acne
has been thought of as a multifactorial disease of
the folliculosebaceous unit, involving excess
sebum production, abnormal follicular
hyperkeratinization, overgrowth of
Propionibacterium acnes, and inflammation (Fig
2). Recent laboratory and clinical investigations
into the roles of the innate immune system and
extracellular matrix remodeling proteins have shed
additional light on this pathogenetic process (5-7).
Role of androgens: Activity of type 1 5areductase
enzyme was shown to predominate in
human sebaceous glands and epidermis. This
enzyme is responsible for the conversion of
testosterone to the more potent androgen,
dihydrotestosterone (DHT). DHT in turn is thought
to mediate androgen dependent skin diseases such
as acne, hirsutism and androgenetic alopecia (13)
The enzyme 5a-reductase type 1 has been studied
in those with and without acne and it has been
hypothesized that those with acne might have more
active 5a-reductase type 1 .(2)
Conclusion : The prominent role of hormones in
the pathophysiology of acne has long been
recognized and corroborated by clinical and
experimental observations and therapeutic
experience (14). Although acne is not considered a
primary endocrine disorder, androgens, such as
dihydrotestosterone, dehydroepiandrosterone
sulfate, and testosterone, and growth hormone and
insulin-like growth factors, have all been
implicated in the pathogenesis of acne (15).
Corresponding address to :
Dr. Yasir Mansour Mohamed Al-Ani
Islam Mohammad Nabil El Helou
Leucine amino peptidases (LAP; EC 3.4.11.1) constitute a diverse set of exopeptidases that catalyze the hydrolysis of leucine residues from the amino-terminal of protein or peptide substrates, (LAP) are present in animals, plants, and microbes. In this study, leucine amino peptidase was purified partial from Arachis hypogaea seeds by using gel filtration chromatography Sephadex G-100. The enzyme was purified 3.965 fold with a recovery of 29.4%. Its pH and temperature optimum were(8.7) and (37oC), respectively. The results show novel properties of LAP from Arachis hypogaea L. or peanut. The Km value for LAP (77 mM), with V max (1538 m mole min-1). We recommend a separate isoenzymeof the enzyme (LAP) from Arachis hypogaea on L. peanut seeds a
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