Changes in distribution and molecular weight of the acrosomal protein acrin2 (MC41) during guinea pig spermiogenesis and epididymal maturation

2001 ◽  
Vol 303 (2) ◽  
pp. 253-261 ◽  
Author(s):  
Kazuya Yoshinaga ◽  
Ichiro Tanii ◽  
Tadasuke Oh-oka ◽  
Kiyotaka Toshimori
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Epididymal Maturation

Immunocytochemical alterations in the intra-acrosomal antigen MN7 during epididymal maturation of guinea pig spermatozoa

1998 ◽  
Vol 292 (2) ◽  
pp. 427-433 ◽  
Author(s):  
K. Yoshinaga ◽  
I. Tanii ◽  
D. K. Saxena ◽  
K. Toshimori
Keyword(s):  
Guinea Pig ◽  
Epididymal Maturation

scholarly journals Separation and partial characterization of guinea-pig caseins

1978 ◽  
Vol 173 (2) ◽  
pp. 633-641 ◽  
Author(s):  
R K Craig ◽  
D McIlreavy ◽  
R L Hall
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Exchange Chromatography

1. Guinea-pig caseins A, B and C were purified free of each other by a combination of ion-exchange chromatography and gel filtration. 2. Determination of the amino acid composition showed all three caseins to contain a high proportion of proline and glutamic acid, but no cysteine. This apart, the amino acid composition of the three caseins was markedly different, though calculated divergence values suggest that some homology may exist between caseins A and B. Molecular-weight estimates based on amino acid composition were in good agreement with those based on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. N-Terminal analysis showed lysine, methionine and lysine to be the N-terminal residues of caseins A, B and C respectively. 4. Two-dimensional separation of tryptic digests revealed a distinctive pattern for each casein. 5. All caseins were shown to be phosphoproteins. The casein C preparation also contained significant amounts of sialic acid, neutral and amino sugars. 6. The results suggest that each casein represents a separate gene product, and that the low-molecular-weight proteins are not the result of a post-translational cleavage of the largest. All were distinctly different from the whey protein alpha-lactalbumin.

scholarly journals The biliary excretion of anions of molecular weight 300-800 in the rat, guinea pig and rabbit

1971 ◽  
Vol 125 (2) ◽  
pp. 25P-26P ◽  
Author(s):  
F T Aziz ◽  
P C Hirom ◽  
P Millburn ◽  
R L Smith ◽  
R T Williams
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Biliary Excretion

An assessment of antigenic potential of β-lactam antibiotics, low molecular weight drugs, using guinea pig models

Toxicology ◽  
1997 ◽  
Vol 123 (1-2) ◽  
pp. 149-160 ◽  
Author(s):  
Hiroyuki Hattori ◽  
Fumie Yamaguchi ◽  
Nobuhiko Wagai ◽  
Michiyuki Kato ◽  
Mamoru Nomura
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Low Molecular Weight

scholarly journals Bioorganic studies on the venom from duckbill platypus

2012 ◽  
Vol 84 (6) ◽  
pp. 1317-1328 ◽  
Author(s):  
Masaki Kita
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Structure And Function ◽  
Low Molecular Weight ◽  
Tissue Kallikrein ◽  
Guinea Pig Ileum ◽  
Porcine Pancreas ◽  
Human Neuroblastoma ◽  
Ornithorhynchus Anatinus ◽  
And Function

Venomous mammals are rare, and only a few species in the orders Insectivora and Monotremata produce toxic venom. Among them, the duckbill platypus (Ornithorhynchus anatinus) is one of the two venomous Australian mammals. The adult male platypus carries a spur on each hind leg, which it uses to inject competitors with poison. However, the structure and function of the poison’s active compounds are still imcompletely characterized. We found that crude platypus venom produced potent Ca2+influx in human neuroblastoma IMR-32 cells. Guided by this assay, we identified 11 unique peptides, including peptide H–His–Asp–His–Pro–Asn–Pro–Arg–OH, which coincided with the N-terminal domain residues ofOrnithorhynchusvenom C-type natriuretic peptide (OvCNP). This heptapeptide induced a significant increase in [Ca2+]iin IMR-32 cells at 75 μM; had relatively specific affinities for glutamate, histamine, and GABAAreceptors; and facilitated neurogenic twitching in guinea pig ileum specimens at 30 μM. We also established that its proteinous venom fraction strongly hydrolyzed Pro–Phe–Arg–MCA and cleaved a human low-molecular-weight kininogen (LK), similar to porcine pancreas kallikrein. These results strongly indicated that platypus venom contains tissue kallikrein-like protease(s), and its proteolytic activity might synergistically contribute to toxicity through the specific cleavage of other venom constituents.

PROTEOGLYCANS AND SULFATED PROTEINS OF PLATELETS: CHARACTERIZATION AND RESPONSE TO THROMBIN AND ADP

1987 ◽  
Author(s):  
B P Schick ◽  
C J Walsh ◽  
T Jenkins-West
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Platelet Activation ◽  
Negative Charge ◽  
Total Cell ◽  
Low Molecular Weight ◽  
Sds Page ◽  
Form Part ◽  
Triton X

The proteoglycans (PG) and sulfated proteins of guinea pig platelets were labeled in vivo by intraperitoneal injection of (35S)sulfate. At 3 days after injection, platelets contained 3 distinct populations of chondroitin-6-sulfate proteoglycans which together constitute about 65% of the cellular (35S) label. Most PG elute from a DEAE-Sephacel column with 4M Gdn HC1 (PG-1, 87%), and elute at Kav 0.12 on Sepharose CL-6B. The PG-1 can be resolved by SDS-PAGE into two fractions. The remainder (PG-2, 13%) elutes from the DEAE-Sephacel column with 4M Gdn HCl/2% Triton X-100 or 2% CHAPS, and has a Kav of 0.07 on Sepharose CL-6B. About 20-25% of the cell (35S) label elutes from DEAE-Sephacel in the wash-through or with 0.23M NaCl, and can be resolved by SDS-PAGE into at least 8 distinct bands which we have tentatively characterized as sulfated glycoproteins. The remainder of the (35S) is in low molecular weight (LMW) material which does not adhere to DEAE-Sephacel and has not been further characterized.Platelets were treated with either thrombin or ADP, and the cells were then separated from the supernatant by centrifugation. The radiolabeled molecules in the supernatant and the cells were analyzed by DEAE-Sephacel and Sepharose CL-6B column chromatography. About 65% of the total cell (35S) was released from the cells by thrombin. Most of this radiolabel adhered to the DEAE-Sephacel column, and was found to be PG-1. The remainder of the released (35S) was about half the LMW material. In contrast, only 10-15% of the (35S)labeled material retained by the cells adhered to DEAE-Sephacel and was found to be PG-2. The remainder of the (35S)-labeled material retained by the platelets was the sulfated proteins and the LMW material. ADP caused release of about 15% of the (35S), and this was found to be in part PG-1 and in part the LMW material, but not PG-2. None of the (35S)-labeled molecules appeared to be degraded during platelet activation. We suggest that the PG-1 represent the a-granule and PG-2 the membrane proteoglycans. The sulfated proteins have not been described previously. Their role is not known, but we hypothesize that they may form part of the negative charge of the glycocalix and thus be part of the reactive surface of the platelet.

Low molecular weight iron in guinea pig reticulocytes

1985 ◽  
Vol 19 (1) ◽  
pp. 75-84 ◽  
Author(s):  
Simeon Pollack ◽  
Theresa Campana ◽  
Janet Weaver
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Low Molecular Weight ◽  
Low Molecular Weight Iron
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