Isolation and Characterization of Messenger Ribonucleic Acid Species for Guinea-Pig Milk Proteins from Free and Membrane-Bound Polyribosomes

1976 ◽  
Vol 4 (2) ◽  
pp. 340-341 ◽  
Author(s):  
OLGA S. HARRISON ◽  
ROGER K. CRAIG ◽  
PETER N. CAMPBELL
Keyword(s):  
Guinea Pig ◽  
Ribonucleic Acid ◽  
Milk Proteins ◽  
Messenger Ribonucleic Acid ◽  
Isolation And Characterization ◽  
Membrane Bound

scholarly journals Isolation and characterization of a membrane protein from rat erythrocytes which inhibits lysis by the membrane attack complex of rat complement

1992 ◽  
Vol 284 (1) ◽  
pp. 169-176 ◽  
Author(s):  
T R Hughes ◽  
S J Piddlesden ◽  
J D Williams ◽  
R A Harrison ◽  
B P Morgan
Keyword(s):  
Affinity Purification ◽  
Membrane Attack Complex ◽  
Erythrocyte Membranes ◽  
Dependent Manner ◽  
Inhibitory Protein ◽  
Rat Erythrocytes ◽  
Butanol Extract ◽  
Isolation And Characterization ◽  
Membrane Bound

The membrane attack complex (MAC) of complement in humans is regulated by several membrane-bound proteins; however, no such proteins have so far been described in other species. Here we report the isolation and characterization of a rat erythrocyte membrane glycoprotein of molecular mass 21 kDa which inserts into cell membranes and is a potent inhibitor of the rat MAC. This protein, here called rat inhibitory protein (RIP), was first partially purified by column chromatography from a butanol extract of rat erythrocyte membranes. Monoclonal antibodies (Mabs) were raised against RIP and used for its affinity purification. Affinity-purified RIP was shown to inhibit in a dose-dependent manner the cobra venom factor (CVF)-mediated ‘reactive’ lysis of guinea pig erythrocytes by rat complement. Conversely, the anti-RIP MAbs 6D1 and TH9 were shown to markedly enhance the CVF-mediated lysis of rat erythrocytes by rat complement. RIP acted late in the assembly of the MAC (at or after the C5b-8 stage) and was releasable from the membranes of rat erythrocytes by phosphatidylinositol-specific phospholipase C. These features, together with its size, deglycosylation pattern and N-terminal amino acid sequence, lead us to conclude that RIP is the rat homologue of the human MAC-inhibitory protein CD59 antigen.

scholarly journals Isolation and characterization of the dopa decarboxylase gene of Drosophila melanogaster

1981 ◽  
Vol 1 (6) ◽  
pp. 475-485
Author(s):  
J Hirsh ◽  
N Davidson
Keyword(s):  
Drosophila Melanogaster ◽  
Ribonucleic Acid ◽  
Deoxyribonucleic Acid ◽  
Isolation Procedure ◽  
Chromosome Band ◽  
Dopa Decarboxylase ◽  
Developmental Profile ◽  
Isolation And Characterization

We have isolated chromosomal deoxyribonucleic acid clones containing the Drosophila dopa decarboxylase gene. We describe an isolation procedure which can be applied to other nonabundantly expressed Drosophila genes. The dopa decarboxylase gene lies within or very near polytene chromosome band 37C1-2. The gene is interrupted by at least one intron, and the primary mode of regulation is pretranslational. At least two additional sequences hybridized by in vivo ribonucleic acid-derived probes are found within a 35-kilobase region surrounding the gene. The developmental profile of ribonucleic acid transcribed from one of these regions differs from that of the dopa decarboxylase transcript.

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