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RGT 1 RGT 2
METH
COMPONENT FUNCTION COMPONENT FUNCTION
Imidazole / Good’s Buffer ● (pH 6.8 – 6.9) Imidazole/Good’s buffer ● (pH 6.8 – 6.9)
(120mmol/L) ● Buffer (90mmol/L) ● Buffer
● Coenzyme ● Substrate
NADP ● Hydrogen acceptor Creatine phosphate ● Source of phosphate on the first
(2.5mmol/L) ● 3rd reaction; come from vitamin (150mmol/L) rxn
B (niacin)
2nd rxn
● Coenzyme
Pyridoxal-5-phosphate ● Accepts amino acid and transfer
(13mmol/L) it to COO- in alpha keto acid
● Active form of vitamin B6
Pyridoxal-5-phosphate ● Coenzyme
(13mmol/L)
● Cofactor ● 4,6-ethylidene-(G7)-p-nitrophe
nyl-(G1)-α-D-maltoheptaoside
(EPS-G7) OR ETHYLIDINE
NaCl EPS-G7
PROTECTED SUBSTRATE
(62.5mmol/L) (8.5mmol/L)
● Substrate
● Prevent interference of residual
AMS activity
α-AMYLASE
● Cofactor
Complete Color
● Activator
Fluid Stable
● Sources of chloride which serves
Mg2Cl
as allosteric activator (changes
(12.5mmol/L)
spatial configuration of the
enzyme for better substrate
binding)
● Indicator enzyme
● Auxiliary enzymes
α-glucosidase
● Redox enzymes
(≥ 2kU/L)
● Acts as a conjunction with the
protein enzyme
LEGEND:
▀ Substrate ▀ Buffer ▀ Indicator ▀ Coenzyme ▀ Activator ▀ Cofactor
Colipase ● Coenzyme ●
(2.2mg/L)
● Activator
Zinc sulfate ● Has high affinity for binding
(0.5mmol/L) (10x) to magnesium if in excess
● Source of zinc
Alkaline
Phosphatase ● Metal ion buffer
Fluid Stable ● Chelating agent
● Binds with zinc & magnesium
(inhibits zinc if in excess)
● Metal ions which buffers the
HEDTA
system to maintain optimal
(2.5mmol/L)
concentration of your zinc and
magnesium; the metal ion buffer
also chelates their potential
inhibitory ions which may be
present in the sample
LEGEND:
▀ Substrate ▀ Buffer ▀ Indicator ▀ Coenzyme ▀ Activator ▀ Cofactor
BUFFERS AND pH
METHODOLOGY BUFFER pH
CK-MB FS
Imidazole / Good’s Buffer 6.8 - 6.9 (nice)
Oliver Rosalki
LDH FS
N-methyl-D-glucamine 8.8 - 8.9
Amador et al, Wacker, Ulmer, Valle
α-AMYLASE
Good’s buffer 7.15
Complete Color Fluid Stable
Alkaline Phosphatase
HEDTA
Fluid Stable