J. Margolis

Australian Red Cross Lifeblood

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

K.G. Kenrick

University of Otago

C.W. Wrigley

Agriculture and Food

P. Rhoades

Orthopedic Center

Z. Stephen Horvath

Macquarie University

Garry L. Corthals

University of Amsterdam

Elizabeth Bishop

Plum Island Animal Disease Center

Sally Bruce

University of Bradford

Keith L. Williams

Macquarie University

Michael Eisen

Australian Red Cross Lifeblood

Wrigley Cw

Commonwealth Scientific and Industrial Research Organisation

Cooperative Institutions

Children's Hospital at Westmead

University of Sydney

Commonwealth Scientific and Industrial Research Organisation

Australian Red Cross Lifeblood

Royal Prince Alfred Hospital

Children's Medical Research Institute

Plant Industry

Macquarie University

UNSW Sydney

Quality Research

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Initiation of blood coagulation by glass and related surfaces

The Journal of Physiology (1957)

J. Margolis

10.1113/jphysiol.1957.sp005799

Cite

Citations (116)

Interrelations Between Different Mechanisms of Release of Biologically Active Peptides from Blood Plasma

Nature (1962)

J. Margolis Elizabeth Bishop

10.1038/194749a0

Cite

Citations (27)

Glass Surface and Blood Coagulation

Nature (1956)

J. Margolis

Diluent

Clotting time

Clotting factor

10.1038/178805b0

Cite

Citations (52)

STUDIES ON PLASMA KININS

Immunology and Cell Biology (1963)

Elizabeth Bishop J. Margolis

SUMMARY The kinin‐destroying enzyme in human plasma is inhibited by metal‐binding compounds, e.g. EDTA, and also by analogues of arginine. Inhibition by EDTA appears to involve chelation of a metal on which the enzyme is dependent. The enzyme can be reactivated by a small group of metal cations (zinc, cadmium, cobalt), although other ions of similar size can be utilised to some extent. The inhibition by arginine and its analogues may be competitive. This is in keeping with the proposed carboxypeptidase nature of the enzyme.

Enzyme Inhibition

10.1038/icb.1963.30

Cite

Citations (9)

An improved procedure for accurate assays of factor VIII

Pathology (1979)

J. Margolis

Calculator

Table (database)

10.3109/00313027909061940

Cite

Citations (12)

Phenotypic expression of the Hp2Hp1 genotype

Biochemical and Biophysical Research Communications (1969)

Jared Sheridan K.G. Kenrick J. Margolis

Expression (computer science)

10.1016/0006-291x(69)90370-2

Cite

Citations (10)

Practical system for ployacrylamide gradient gel electrophoresis.

PubMed (1973)

J. Margolis

Source

Cite

Citations (2)

Quantitative Studies of Kinin-Releasing Enzymes in Plasma

Springer eBooks (1966)

J. Margolis

10.1007/978-3-642-94965-4_20

Cite

Citations (6)

Multifunctional apparatus for electrokinetic processing of proteins

Electrophoresis (1994)

Z. Stephen Horvath Garry L. Corthals C.W. Wrigley J. Margolis

Abstract New equipment (the “Gradiflow TM ”) has been designed and constructed to provide efficient large‐scale preparative fractionation of macromolecules, based on charge and/or size differences, as well as the concentration of macromolecules and electrodialysis. Examples of its capability are the separation of a mixture of haemoglobin (50 mg) from bovine serum albumin (50 mg) within 15 min (based on charge differences at pH 6.8), the purification of phycoerythrin from a crude extract on the basis of size, and the fractionation of serum proteins into two discrete size classes.

Bovine serum albumin

10.1002/elps.11501501141

Cite

Citations (65)

The mode of action of Hageman factor in the release of plasma kinin

The Journal of Physiology (1960)

J. Margolis

10.1113/jphysiol.1960.sp006434

Cite

Citations (100)