مُحللـون / Analysts
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نداء لممثل المسائي الاخ حسين كاري
راسل ست رسل على المخطط الاخي الموجود بالخامسة
احنه ست زهراء تركته النه
اخوان الرابعة
مخطط الاخير بالمختبر الخامس اخر ورقة ترك
والمختبر الرابعة تبع الكمبتتف والنن كمبتتف مطلوبات
ماكو شي ترك بالشرحيات
Repost from N/a
Q//4 / A
Increase of velocity with temperature, but
Decrease of velocity with higher temperature.
Repost from N/a
Q//4 / B
3. The pH optimum varies for different enzymes. For example, pepsin,
a digestive enzyme in the stomach, is maximally active at pH 2,
whereas other enzymes, designed to work at neutral pH, are
denatured by such an acidic environment.
Repost from N/a
Q//3
V⁰= Vmax [S] / Km + [S]
- Describe how velocity of reaction varies with substrate concentration .
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Q/2
1- energy changes during reaction and chemistry of active site.
2- (40 C°).
3- enzyme - substrate (ES) complex .
4- Active site .
5- Substrate binding and catalysis.
6- (10³ - 10⁸).
7- Apoenzyme.
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Q//4
1- Diagnosis infectious diseases .
2- to diagnose due to its sensitivity and specificity.
3- (45nm).
4- Enzyme - linked immunosorbent assay.
5- come in several forms.
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Q//2
A//
1. The Regulation: Allosteric enzymes are regulated by molecules called
effectors (also called modifiers) that bind noncovalently at a site other than
the active site.
2. These enzymes are usually composed of multiple subunits, and the
regulatory (allosteric) site that binds the effector may be located on a subunit
that is not itself catalytic.
3. The presence of an allosteric effector can alter the affinity of the enzyme for
its substrate, or modify the maximal catalytic activity of the enzyme, or
both.
4. Effectors can be either positive (accelerate the enzyme-catalyzed reaction)
or negative (slow down the reaction) .
5. Allosteric enzymes frequently catalyze the committed step (slowest step) of a
pathway.
B// Electrophoresis (Def.) is a laboratory technique used to separate DNA, RNA or
protein molecules based on their size and electrical charge. An electric current is
used to move the molecules through a gel or other matrix.
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+1
Q//1
●Competitive inhibition
This type of inhibition occurs when the inhibitor binds reversibly to the
same site that the substrate would normally occupy and, therefore, competes
with the substrate for that site.
●Noncompetitive inhibition occurs when the inhibitor and substrate
bind at different sites on the enzyme.
Repost from مُحللـون / Analysts
انزيمات عملي / شهر اول
مسائي
الاول/ صح وخطا وصحح الخطا 5 نقاط
الثاني/ 1)قانون Lineweaver-Burk plot ونوضح الي بالقانون مثلًا الـ vmax شنو معناها وغيرها من الرموز
.
2) why we should study the initial velocity ?
السؤال الثالث / Enumerate and explain factor that effect on velocity؟
جوابهن
حراره وتركيز و ph مع التوضيح
