Local hydrogen-clearance and PO2-measurements in micro-areas of the rat brain.
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Animals↗
Biomedical subjects
H Metzger
Publications and source records attributed to H Metzger.
Affinity labeling of a mouse myeloma protein which binds nitrophenyl ligands. Kinetics of labeling and isolation of a labeled peptide.
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Amino Acids↗
[Biochemistry of some parasitic helminths and protozoa and the mode of action of some antiparasitic drugs].
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Adenosine Triphosphate↗
Human IgA-myeloma protein which binds nitrophenyl ligands.
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Aminocaproates↗
Structure and function of gamma M macroglobulins.
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Amino Acids↗
[Influence of the particle penetration trajectory on the volume distribution curve, according to the Coulter principle].
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Blood Cell Count↗
Catabolism of pteridine cofactors. I. Properties and metabolism in rat liver homogenates of tetrahydrobiopterin and tetrahydroneopterin.
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Animals↗
A Waldenström macroglobulin which binds nitrophenyl ligands.
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Amino Acids↗
Medical problems of civil disorders. Organization of a volunteer group of health professionals to provide medical services in a riot.
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Aggression↗
[O2 exchange between capillaries and tissue. II. O2 concentration profiles in homogenous and nonhomogenous blood flow of two dimensional capillary models].
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Capillaries↗
Myeloma proteins and antibodies.
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Antibody Formation↗
Partial sequences of six macroglobulin light chains. Absence of sequence correlates to functional activity.
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Amino Acid Sequence↗
The specificity of a monoclonal macroglobulin (gamma M) antibody: reactivity with primate gamma G immunoglobulins.
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Animals↗
[Changes in regional oxygen partial pressure following sudden changes in the inspiratory O2 concentration].
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Animals↗
[H2-clearance and pO2-measurements in the brain tissue of rats and cats with the same Pt-microelectrode].
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Animals↗
[pO2-fields in homogeneously and inhomogeneously perfused 2-dimensional tissue models].
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Blood Flow Velocity↗
Affinity site labeling of a mouse myeloma protein which binds dinitrophenyl ligands.
A mouse myeloma protein of the immunoglobulin A class, which specifically binds dinitrophenyl ligands, has been successfully affinity labeled (site-directed labeling) with several diazonium reagents, leading to inactivation of the combining sites. The labeling reagents reacted only with tyrosine residues of light chain origin. The 7S subunit of the myeloma protein appears to contain only one reactive site.
Animals↗