Characterization of antibody against human liver guanase by immunoblotting and immunohistochemical staining of human liver guanase by a direct labeling antibody-enzyme method.

Human liver guanase was purified and a specific antibody against it was raised in rabbits. The antiserum formed a single precipitin line with human liver extract, and also completely inhibited the activity of the liver enzyme. An immunoblotting study showed that the antibody bound specifically to one band of protein with guanase activity and not to other proteins. Therefore, we concluded that this antiserum against the liver enzyme was suitable for use in immunohistochemical demonstration of guanase. In tissue sections, the immunohistochemical reaction with this antibody was positive in the same locations as the histochemical guanase reaction with DAB (3,3'-diaminobenzidine tetrahydrochloride).

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Recent advances in the detection and characterization of specific antibody-forming cells in tissue sections

The Histochemical Journal ◽

10.1007/bf01675613 ◽

1986 ◽

Vol 18 (9) ◽

pp. 465-471 ◽

Cited By ~ 19

Author(s):

N. Van Rooijen ◽

E. Claassen

Keyword(s):

Specific Antibody ◽

Tissue Sections ◽

Recent Advances

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Immunological characterization of human liver α-D-mannosidase

Biochemical Journal ◽

10.1042/bj1510469a ◽

1975 ◽

Vol 151 (3) ◽

pp. 469-475 ◽

Cited By ~ 15

Author(s):

N Phillips ◽

D Robinson ◽

B Winchester

Keyword(s):

Human Brain ◽

Human Plasma ◽

Human Liver ◽

Double Diffusion ◽

Immunological Characterization ◽

Precipitin Line ◽

Structural Resemblance ◽

Optimum Ph

Antiserum was raised against purified human liver α-D-mannosidase B. It precipitated α-mannosidases A and B from solution, demonstrating the close structural resemblance of these 2 forms of acidic α-mannosidase activity. A continuous enzymically active precipitin line with no spurs was obtained when α-mannosidase A and B were placed in adjacent wells on Ouchterlony double-diffusion plates. The antiserum precipitated acidic but not neutral α-mannosidase from an extract of human liver, confirming that the acidic and neutral activities are not closely related. Acidic activity was also precipitated from extracts of human brain, kidney and leucocytes by the antiserum. However, it did not cross-react with bovine acidic α-mannosidase activity or with the activity in human plasma that has an optimum pH of 5.5. The two acidic forms of human liver α-mannosidase, A and B, are immunologically identical but distinct from neutral α-mannosidase and that activity with an optimum pH of 5.5.

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Uridine diphosphate glucose pyrophosphorylase: differential heat inactivation and further characterization of human liver enzyme

Biochimica et Biophysica Acta (BBA) - Enzymology ◽

10.1016/0005-2744(74)90132-6 ◽

1974 ◽

Vol 364 (1) ◽

pp. 59-67 ◽

Cited By ~ 8

Author(s):

Richard L. Turnquist ◽

Marlys M. Turnquist ◽

Robert C. Bachmann ◽

R.Gaurth Hansen

Keyword(s):

Liver Enzyme ◽

Human Liver ◽

Heat Inactivation ◽

Uridine Diphosphate ◽

Differential Heat ◽

Uridine Diphosphate Glucose ◽

Diphosphate Glucose

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Immunochemical characterization of monoamine oxidase from human liver, placenta, platelets and brain cortex

Biochemical Journal ◽

10.1042/bj1810015 ◽

1979 ◽

Vol 181 (1) ◽

pp. 15-20 ◽

Cited By ~ 16

Author(s):

S M Russell ◽

J Davey ◽

R J Mayer

Keyword(s):

Enzyme Activity ◽

Monoamine Oxidase ◽

Liver Enzyme ◽

Human Liver ◽

Brain Cortex ◽

Lipid Binding ◽

Mitochondrial Preparation ◽

Immunochemical Characterization ◽

Immunodiffusion Analysis

1. Antiserum raised to purified human liver monoamine oxidase was used to characterize the monoamine oxidase from human liver, brain cortex, placenta and platelets. 2. Antibodies to monoamine oxidase were purified by adsorption with a mitochondrial preparation. 3. Monoamine oxidase was present in liver particle-free supernatant as measured by enzyme activity and immunodiffusion. 4. Multiple precipitin lines were obtained on immunodiffusion analysis against the purified liver enzyme. It is proposed that this is due to either aggregation or to differential lipid binding. 5. The results suggest that the functionally different enzymes found in liver, brain cortex, platelets and placenta are immunochemically related and may be identical.

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